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|nmr structure of yeast oligosaccharyltransferase subunit ost4p|
In molecular biology, OST4 (Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 4) is a subunit of the oligosaccharyltransferase complex. OST4 is a very short, approximately 30 amino acids, protein found from fungi to vertebrates. It appears to be an integral membrane protein that mediates the en bloc transfer of a pre-assembled high-mannose oligosaccharide onto asparagine residues of nascent polypeptides as they enter the lumen of the rough endoplasmic reticulum.
- Kelleher DJ, Gilmore R (2006). "An evolving view of the eukaryotic oligosaccharyltransferase.". Glycobiology 16 (4): 47R-62R. doi:10.1093/glycob/cwj066. PMID 16317064. http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=16317064.
- Gayen S, Kang C (2011). "Solution structure of a human minimembrane protein Ost4, a subunit of the oligosaccharyltransferase complex.". Biochem Biophys Res Commun 409 (3): 572–6. doi:10.1016/j.bbrc.2011.05.050. PMID 21609714. http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=21609714.
- Spirig U, Bodmer D, Wacker M, Burda P, Aebi M (2005). "The 3.4-kDa Ost4 protein is required for the assembly of two distinct oligosaccharyltransferase complexes in yeast.". Glycobiology 15 (12): 1396–406. doi:10.1093/glycob/cwj025. PMID 16096346. http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=16096346.
Oligosaccaryltransferase Provide feedback
Ost4 is a very short, approximately 30 residues, enzyme found from fungi to vertebrates. It is a member of the ER oligosaccaryltansferase complex, EC 22.214.171.124, that catalyses the asparagine-linked glycosylation of proteins. It appears to be an integral membrane protein that mediates the en bloc transfer of a preassembled high-mannose oligosaccharide onto asparagine residues of nascent polypeptides as they enter the lumen of the rough endoplasmic reticulum (RER).
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR018943
Ost4 is a very short, approximately 30 residues, enzyme found from fungi to vertebrates. It is a member of the ER oligosaccaryltansferase complex, EC, that catalyses the asparagine-linked glycosylation of proteins. It appears to be an integral membrane protein that mediates the en bloc transfer of a pre-assembled high-mannose oligosaccharide onto asparagine residues of nascent polypeptides as they enter the lumen of the rough endoplasmic reticulum.
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This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
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Curation and family details
|Seed source:||Wood V|
|Author:||Wood V, Coggill P|
|Number in seed:||12|
|Number in full:||156|
|Average length of the domain:||34.50 aa|
|Average identity of full alignment:||44 %|
|Average coverage of the sequence by the domain:||50.21 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||4|
|Download:||download the raw HMM for this family|
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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 Ost4 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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