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2  structures 2012  species 1  interaction 3379  sequences 136  architectures

Family: CheR_N (PF03705)

Summary: CheR methyltransferase, all-alpha domain

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This is the Wikipedia entry entitled "Protein-glutamate O-methyltransferase". More...

Protein-glutamate O-methyltransferase Edit Wikipedia article

protein-glutamate O-methyltransferase
Identifiers
EC number 2.1.1.80
CAS number 9055-09-8
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO
CheR methyltransferase, all-alpha domain
PDB 1bc5 EBI.jpg
chemotaxis receptor recognition by protein methyltransferase cher
Identifiers
Symbol CheR_N
Pfam PF03705
InterPro IPR022641
SCOP 1af7
SUPERFAMILY 1af7
CheR methyltransferase, SAM binding domain
PDB 1bc5 EBI.jpg
chemotaxis receptor recognition by protein methyltransferase cher
Identifiers
Symbol CheR
Pfam PF01739
Pfam clan CL0063
InterPro IPR022642
SCOP 1af7
SUPERFAMILY 1af7

In enzymology, a protein-glutamate O-methyltransferase (EC 2.1.1.80) is an enzyme that catalyzes the chemical reaction

S-adenosyl-L-methionine + protein L-glutamate \rightleftharpoons S-adenosyl-L-homocysteine + protein L-glutamate methyl ester

Thus, the two substrates of this enzyme are S-adenosyl methionine and protein L-glutamic acid, whereas its two products are S-adenosylhomocysteine and protein L-glutamate methyl ester.

This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:protein-L-glutamate O-methyltransferase. Other names in common use include methyl-accepting chemotaxis protein O-methyltransferase, S-adenosylmethionine-glutamyl methyltransferase, methyl-accepting chemotaxis protein methyltransferase II, S-adenosylmethionine:protein-carboxyl O-methyltransferase, protein methylase II, MCP methyltransferase I, MCP methyltransferase II, protein O-methyltransferase, protein(aspartate)methyltransferase, protein(carboxyl)methyltransferase, protein carboxyl-methylase, protein carboxyl-O-methyltransferase, protein carboxylmethyltransferase II, protein carboxymethylase, protein carboxymethyltransferase, and protein methyltransferase II. This enzyme participates in bacterial chemotaxis - general and bacterial chemotaxis - organism-specific.

CheR proteins are part of the chemotaxis signaling mechanism which methylates the chemotaxis receptor at specific glutamate residues. Methyl transfer from the ubiquitous S-adenosyl-L-methionine (AdoMet/SAM) to either nitrogen, oxygen or carbon atoms is frequently employed in diverse organisms ranging from bacteria to plants and mammals. The reaction is catalysed by methyltransferases (Mtases) and modifies DNA, RNA, proteins and small molecules, such as catechol for regulatory purposes. The various aspects of the role of DNA methylation in prokaryotic restriction-modification systems and in a number of cellular processes in eukaryotes including gene regulation and differentiation is well documented.

Flagellated bacteria swim towards favourable chemicals and away from deleterious ones. Sensing of chemoeffector gradients involves chemotaxis receptors, transmembrane (TM) proteins that detect stimuli through their periplasmic domains and transduce the signals via their cytoplasmic domains .[1] Signalling outputs from these receptors are influenced both by the binding of the chemoeffector ligand to their periplasmic domains and by methylation of specific glutamate residues on their cytoplasmic domains. Methylation is catalysed by CheR, an S-adenosylmethionine-dependent methyltransferase,[1] which reversibly methylates specific glutamate residues within a coiled coil region, to form gamma-glutamyl methyl ester residues.[1][2] The structure of the Salmonella typhimurium chemotaxis receptor methyltransferase CheR, bound to S-adenosylhomocysteine, has been determined to a resolution of 2.0 Angstrom.[1] The structure reveals CheR to be a two-domain protein, with a smaller N-terminal helical domain linked via a single polypeptide connection to a larger C-terminal alpha/beta domain. The C-terminal domain has the characteristics of a nucleotide-binding fold, with an insertion of a small anti-parallel beta-sheet subdomain. The S-adenosylhomocysteine-binding site is formed mainly by the large domain, with contributions from residues within the N-terminal domain and the linker region.[1]

Structural studies[edit]

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1AF7 and 1BC5.

References[edit]

  1. ^ a b c d e Djordjevic S, Stock AM (April 1997). "Crystal structure of the chemotaxis receptor methyltransferase CheR suggests a conserved structural motif for binding S-adenosylmethionine". Structure 5 (4): 545–58. doi:10.1016/S0969-2126(97)00210-4. PMID 9115443. 
  2. ^ Djordjevic S, Stock AM (June 1998). "Chemotaxis receptor recognition by protein methyltransferase CheR". Nat. Struct. Biol. 5 (6): 446–50. doi:10.1038/nsb0698-446. PMID 9628482. 

Further reading[edit]

  • Burgess-Cassler A, Ullah AH, Ordal GW (1982). "Purification and characterization of Bacillus subtilis methyl-accepting chemotaxis protein methyltransferase II". J. Biol. Chem. 257 (14): 8412–7. PMID 6806296. 
  • Kleene SJ, Toews ML, Adler J (1977). "Isolation of glutamic acid methyl ester from an Escherichia coli membrane protein involved in chemotaxis". J. Biol. Chem. 252 (10): 3214–8. PMID 16888. 
  • Simms SA, Stock AM, Stock JB (1987). "Purification and characterization of the S-adenosylmethionine:glutamyl methyltransferase that modifies membrane chemoreceptor proteins in bacteria". J. Biol. Chem. 262 (18): 8537–43. PMID 3298235. 
  • Springer WR, Koshland DE Jr (1977). "Identification of a protein methyltransferase as the cheR gene product in the bacterial sensing system". Proc. Natl. Acad. Sci. U.S.A. 74 (2): 533–7. doi:10.1073/pnas.74.2.533. PMC 392324. PMID 322131. 

This article incorporates text from the public domain Pfam and InterPro IPR022641

This article incorporates text from the public domain Pfam and InterPro IPR022642

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

CheR methyltransferase, all-alpha domain Provide feedback

CheR proteins are part of the chemotaxis signaling mechanism in bacteria. CheR methylates the chemotaxis receptor at specific glutamate residues. CheR is an S-adenosylmethionine- dependent methyltransferase.

Literature references

  1. Djordjevic S, Stock AM; , Structure 1997;5:545-558.: Crystal structure of the chemotaxis receptor methyltransferase CheR suggests a conserved structural motif for binding S-adenosylmethionine. PUBMED:9115443 EPMC:9115443


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR022641

CheR proteins are part of the chemotaxis signaling mechanism which methylates the chemotaxis receptor at specific glutamate residues. This entry refers to the N-terminal domain of the CherR-type MCP methyltransferases, which are found in bacteria, archaea and green plants. This entry is found in association with .

Methyl transfer from the ubiquitous S-adenosyl-L-methionine (AdoMet) to either nitrogen, oxygen or carbon atoms is frequently employed in diverse organisms ranging from bacteria to plants and mammals. The reaction is catalysed by methyltransferases (Mtases) and modifies DNA, RNA, proteins and small molecules, such as catechol for regulatory purposes. The various aspects of the role of DNA methylation in prokaryotic restriction-modification systems and in a number of cellular processes in eukaryotes including gene regulation and differentiation is well documented.

Three classes of DNA Mtases transfer the methyl group from AdoMet to the target base to form either N-6-methyladenine, or N-4-methylcytosine, or C-5- methylcytosine. In C-5-cytosine Mtases, ten conserved motifs are arranged in the same order [PUBMED:8127644]. Motif I (a glycine-rich or closely related consensus sequence; FAGxGG in M.HhaI [PUBMED:8343957]), shared by other AdoMet-Mtases [PUBMED:2684970], is part of the cofactor binding site and motif IV (PCQ) is part of the catalytic site. In contrast, sequence comparison among N-6-adenine and N-4-cytosine Mtases indicated two of the conserved segments [PUBMED:2690010], although more conserved segments may be present. One of them corresponds to motif I in C-5-cytosine Mtases, and the other is named (D/N/S)PP(Y/F). Crystal structures are known for a number of Mtases [PUBMED:7607476, PUBMED:8343957, PUBMED:8127644, PUBMED:7971991]. The cofactor binding sites are almost identical and the essential catalytic amino acids coincide. The comparable protein folding and the existence of equivalent amino acids in similar secondary and tertiary positions indicate that many (if not all) AdoMet-Mtases have a common catalytic domain structure. This permits tertiary structure prediction of other DNA, RNA, protein, and small-molecule AdoMet-Mtases from their amino acid sequences [PUBMED:7897657].

Flagellated bacteria swim towards favourable chemicals and away from deleterious ones. Sensing of chemoeffector gradients involves chemotaxis receptors, transmembrane (TM) proteins that detect stimuli through their periplasmic domains and transduce the signals via their cytoplasmic domains [PUBMED:9115443]. Signalling outputs from these receptors are influenced both by the binding of the chemoeffector ligand to their periplasmic domains and by methylation of specific glutamate residues on their cytoplasmic domains. Methylation is catalysed by CheR, an S-adenosylmethionine-dependent methyltransferase [PUBMED:9115443], which reversibly methylates specific glutamate residues within a coiled coil region, to form gamma-glutamyl methyl ester residues [PUBMED:9115443, PUBMED:9628482]. The structure of the Salmonella typhimurium chemotaxis receptor methyltransferase CheR, bound to S-adenosylhomocysteine, has been determined to a resolution of 2.0 A [PUBMED:9115443]. The structure reveals CheR to be a two-domain protein, with a smaller N-terminal helical domain linked via a single polypeptide connection to a larger C-terminal alpha/beta domain. The C-terminal domain has the characteristics of a nucleotide-binding fold, with an insertion of a small anti-parallel beta-sheet subdomain. The S-adenosylhomocysteine-binding site is formed mainly by the large domain, with contributions from residues within the N-terminal domain and the linker region [PUBMED:9115443].

Domain organisation

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Full
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Representative proteomes NCBI
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Meta
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RP15
(348)
RP35
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RP55
(867)
RP75
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  Seed
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Full
(3379)
Representative proteomes NCBI
(2654)
Meta
(197)
RP15
(348)
RP35
(678)
RP55
(867)
RP75
(1043)
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Seed source: Pfam-B_694 (release 4.2)
Previous IDs: none
Type: Domain
Author: Bateman A, Griffiths-Jones SR
Number in seed: 77
Number in full: 3379
Average length of the domain: 56.40 aa
Average identity of full alignment: 24 %
Average coverage of the sequence by the domain: 14.23 %

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HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.8 20.8
Trusted cut-off 20.8 20.8
Noise cut-off 20.7 20.7
Model length: 57
Family (HMM) version: 10
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Interactions

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CheR

Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the CheR_N domain has been found. There are 2 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.

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