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InterPro: IPR001264 Glycosyl transferase, family 51

Protein matchesHelp
UniProtKB
Matches:
5133 proteins
AccessionHelp IPR001264 Glyco_trans_51
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Found in IPR011812 Monofunctional biosynthetic peptidoglycan transglycosylase
IPR011813 Penicillin-binding protein 1B
IPR011815 Penicillin-binding protein 1C
IPR011816 Penicillin-binding protein 1A
GO Term annotationHelp
Process GO:0009252 peptidoglycan biosynthetic process
Function GO:0003824 catalytic activity
Component GO:0009274 peptidoglycan-based cell wall
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

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].

Structural linksHelp
SCOP: d.2.1.10
Database linksHelp
Enzyme: EC:2.4.2
CAZy: GT51
PANDIT: PF00912
Blocks: IPB001264

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR001264 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O66874 Penicillin-binding protein 1A

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR011816 Penicillin-binding protein 1A
IPR001264 Glycosyl transferase, family 51
IPR001460 Penicillin-binding protein, transpeptidase
IPR012338 Beta-lactamase-type transpeptidase fold
SWISS-MODEL
PDB Chain
ModBase
SCOP Domain

PublicationsHelp
1. Campbell JA, Davies GJ, Bulone V, Henrissat B.
A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities.
Biochem. J. 326 ( Pt 3) 929-39 1997 [PubMed: 9334165]
http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=9334165
2. Henrissat B, Coutinho PM.
Carbohydrate-Active Enzymes server.
1999
3. Lefevre F, Remy MH, Masson JM.
Topographical and functional investigation of Escherichia coli penicillin-binding protein 1b by alanine stretch scanning mutagenesis.
J. Bacteriol. 179 4761-7 1997 [PubMed: 9244263]
http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=9244263
4. Spratt BG, Zhou J, Taylor M, Merrick MJ.
Monofunctional biosynthetic peptidoglycan transglycosylases.
Mol. Microbiol. 19 639-40 1996 [PubMed: 8830253]
http://dx.doi.org/10.1046/j.1365-2958.1996.442924.x

Additional ReadingHelp
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
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
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
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
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]
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