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22  structures 2  species 0  interactions 4  sequences 1  architecture

Family: T4-Gluco-transf (PF09198)

Summary: Bacteriophage T4 beta-glucosyltransferase

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This is the Wikipedia entry entitled "DNA beta-glucosyltransferase". More...

DNA beta-glucosyltransferase Edit Wikipedia article

DNA beta-glucosyltransferase
Identifiers
EC number 2.4.1.27
CAS number 9030-14-2
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

In enzymology, a DNA beta-glucosyltransferase (EC 2.4.1.27) is an enzyme that catalyzes the chemical reaction in which a beta-D-glucosyl residue is transferred from UDP-glucose to an hydroxymethylcytosine residue in DNA. It is analogous to the enzyme DNA alpha-glucosyltransferase.

This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucose:DNA beta-D-glucosyltransferase. Other names in common use include T4-HMC-beta-glucosyl transferase, T4-beta-glucosyl transferase, T4 phage beta-glucosyltransferase, UDP glucose-DNA beta-glucosyltransferase, and uridine diphosphoglucose-deoxyribonucleate beta-glucosyltransferase.

Structural studies[edit]

As of late 2007, 20 structures have been solved for this class of enzymes, with PDB accession codes 1BGT, 1BGU, 1C3J, 1IXY, 1J39, 1JEJ, 1JG6, 1JG7, 1JIU, 1JIV, 1JIX, 1M5R, 1NVK, 1NZD, 1NZF, 1QKJ, 1SXP, 1SXQ, 2BGT, and 2BGU.

Bacteriophage T4 beta-glucosyltransferase[edit]

T4-Gluco-transf
PDB 1m5r EBI.jpg
ternary complex of t4 phage bgt with udp and a 13 mer dna duplex
Identifiers
Symbol T4-Gluco-transf
Pfam PF09198
InterPro IPR015281
SCOP 1jix
SUPERFAMILY 1jix

In molecular biology,Bacteriophage T4 beta-glucosyltransferase refers to a protein domain found in a virus of Escherichia coli named bacteriophage T4. Members of this family are enzymes encoded by bacteriophage T4, which modify DNA by transferring glucose from uridine diphosphoglucose to 5-hydroxymethyl cytosine bases of phage T4 DNA.[1]

Function[edit]

Beta-glucosyltransferase is an enzyme, or more specifically an inverting glycosyltransferase(GT). In other words it transfers glucose from uridine diphospho-glucose (UDPglucose)to an acceptor, modified DNA through beta-Glycosidic bond. The role of the enzyme is to protect the infecting viral DNA from the bacteria's restriction enzymes. Glucosylation prevents the virus DNA from being cut up. Furthermore, glucosylation may aid gene expression of the bacteriophage by influencing transcription.[2][3][4]

Structure[edit]

This structure has both alpha helices and beta strands.[2]

References[edit]

  1. ^ Moréra S, Larivière L, Kurzeck J, Aschke-Sonnenborn U, Freemont PS, Janin J, Rüger W (August 2001). "High resolution crystal structures of T4 phage beta-glucosyltransferase: induced fit and effect of substrate and metal binding". J. Mol. Biol. 311 (3): 569–77. doi:10.1006/jmbi.2001.4905. PMID 11493010. 
  2. ^ a b Larivière L, Gueguen-Chaignon V, Moréra S (2003). "Crystal structures of the T4 phage beta-glucosyltransferase and the D100A mutant in complex with UDP-glucose: glucose binding and identification of the catalytic base for a direct displacement mechanism.". J Mol Biol 330 (5): 1077–86. PMID 12860129. 
  3. ^ Moréra S, Imberty A, Aschke-Sonnenborn U, Rüger W, Freemont PS (1999). "T4 phage beta-glucosyltransferase: substrate binding and proposed catalytic mechanism.". J Mol Biol 292 (3): 717–30. doi:10.1006/jmbi.1999.3094. PMID 10497034. 
  4. ^ Moréra S, Larivière L, Kurzeck J, Aschke-Sonnenborn U, Freemont PS, Janin J et al. (2001). "High resolution crystal structures of T4 phage beta-glucosyltransferase: induced fit and effect of substrate and metal binding.". J Mol Biol 311 (3): 569–77. doi:10.1006/jmbi.2001.4905. PMID 11493010. 

This article incorporates text from the public domain Pfam and InterPro IPR015281

References[edit]

  • Kornberg SR, Zimmerman SB and Kornberg A (1961). "Glucosylation of deoxyribonucleic acid by enzymes from bacteriophage-infected Escherichia coli". J. Biol. Chem. 236: 1487–1493. 

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Bacteriophage T4 beta-glucosyltransferase Provide feedback

Members of this family are DNA-modifying enzymes encoded by bacteriophage T4 that transfer glucose from uridine diphosphoglucose to 5-hydroxymethyl cytosine bases of phage T4 DNA [1].

Literature references

  1. Morera S, Lariviere L, Kurzeck J, Aschke-Sonnenborn U, Freemont PS, Janin J, Ruger W; , J Mol Biol. 2001;311:569-577.: High resolution crystal structures of T4 phage beta-glucosyltransferase: induced fit and effect of substrate and metal binding. PUBMED:11493010 EPMC:11493010


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR015281

Members of this family are DNA-modifying enzymes encoded by bacteriophage T4 that transfer glucose from uridine diphosphoglucose to 5-hydroxymethyl cytosine bases of phage T4 DNA [PUBMED:11493010].

Domain organisation

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Alignments

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Curation and family details

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Seed source: pdb_1jix
Previous IDs: none
Type: Domain
Author: Sammut SJ
Number in seed: 2
Number in full: 4
Average length of the domain: 38.00 aa
Average identity of full alignment: 82 %
Average coverage of the sequence by the domain: 13.98 %

HMM information View help on HMM parameters

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 25.0 25.0
Trusted cut-off 56.4 55.2
Noise cut-off 17.9 14.8
Model length: 38
Family (HMM) version: 5
Download: download the raw HMM for this family

Species distribution

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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 T4-Gluco-transf domain has been found. There are 22 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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