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InterPro: IPR001264 Glycosyl transferase, family 51
Protein matches
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UniProtKB Matches: 5133 proteins |
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Accession
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IPR001264 Glyco_trans_51 |
Type
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Domain |
Signatures
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InterPro Relationships
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Found in
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IPR011812 Monofunctional biosynthetic peptidoglycan transglycosylase
IPR011813 Penicillin-binding protein 1B
IPR011815 Penicillin-binding protein 1C
IPR011816 Penicillin-binding protein 1A
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GO Term annotation
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Process
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GO:0009252 peptidoglycan biosynthetic process
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Function
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GO:0003824 catalytic activity
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Component
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GO:0009274 peptidoglycan-based cell wall
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InterPro annotation
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Entry Details in BioMart
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Abstract
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The biosynthesis of disaccharides, oligosaccharides and polysaccharides involves the action of hundreds of different glycosyltransferases. These enzymes catalyse the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. A classification of glycosyltransferases using nucleotide diphospho-sugar, nucleotide monophospho-sugar and sugar phosphates (EC:2.4.1.-) and related proteins into distinct sequence based families has been described [1]. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site [2]. The same three-dimensional fold is expected to occur within each of the families. Because 3-D structures are better conserved than sequences, several of the families defined on the basis of sequence similarities may have similar 3-D structures and therefore form 'clans'.
Glycosyltransferase family 51 GT51 comprises enzymes with only one known activity; murein polymerases (EC:2.4). These enzymes utilise MurNAc-GlcNAc-P-P-lipid II as the sugar donor.
The family includes the bifunctional penicillin-binding proteins that have a
transglycosylase (N terminus) and transpeptidase (C terminus) domain [3] and
the monofunctional biosynthetic peptidoglycan transglycosylases [4].
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Structural links
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Database links
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Additional Reading
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Di Guilmi AM, Dessen A, Dideberg O, Vernet T.
The glycosyltransferase domain of penicillin-binding protein 2a from Streptococcus pneumoniae catalyzes the polymerization of murein glycan chains.
J. Bacteriol. 185 2003 4418-23
[PubMed: 12867450]
http://dx.doi.org/10.1128/JB.185.15.4418-4423.2003
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Lovering AL, de Castro LH, Lim D, Strynadka NC.
Structural insight into the transglycosylation step of bacterial cell-wall biosynthesis.
Science 315 2007 1402-5
[PubMed: 17347437]
http://dx.doi.org/10.1126/science.1136611
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Lovering AL, De Castro L, Strynadka NC.
Identification of dynamic structural motifs involved in peptidoglycan glycosyltransfer.
J. Mol. Biol. 383 2008 167-77
[PubMed: 18760285]
http://dx.doi.org/10.1016/j.jmb.2008.08.020
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Yuan Y, Barrett D, Zhang Y, Kahne D, Sliz P, Walker S.
Crystal structure of a peptidoglycan glycosyltransferase suggests a model for processive glycan chain synthesis.
Proc. Natl. Acad. Sci. U.S.A. 104 2007 5348-53
[PubMed: 17360321]
http://dx.doi.org/10.1073/pnas.0701160104
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Yuan Y, Fuse S, Ostash B, Sliz P, Kahne D, Walker S.
Structural analysis of the contacts anchoring moenomycin to peptidoglycan glycosyltransferases and implications for antibiotic design.
ACS Chem. Biol. 3 2008 429-36
[PubMed: 18642800]
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Kelly JA, Kuzin AP, Charlier P, Fonze E.
X-ray studies of enzymes that interact with penicillins.
Cell. Mol. Life Sci. 54 1998 353-8
[PubMed: 9614972]
http://dx.doi.org/10.1007/s000180050163
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InterPro 23.1
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