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PDBsum entry 3bsw

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protein ligands links
Transferase PDB id
3bsw
Jmol
Contents
Protein chain
191 a.a. *
Ligands
CIT
Waters ×206
* Residue conservation analysis
PDB id:
3bsw
Name: Transferase
Title: Pgld-citrate complex, from campylobacter jejuni nctc 11168
Structure: Acetyltransferase. Chain: a. Engineered: yes
Source: Campylobacter jejuni. Strain: nctc 11168. Gene: pgld. Expressed in: escherichia coli.
Resolution:
1.77Å     R-factor:   0.184     R-free:   0.199
Authors: N.B.Olivier,B.Imperiali
Key ref: N.B.Olivier and B.Imperiali (2008). Crystal structure and catalytic mechanism of PglD from Campylobacter jejuni. J Biol Chem, 283, 27937-27946. PubMed id: 18667421
Date:
26-Dec-07     Release date:   29-Jul-08    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q0P9D1  (Q0P9D1_CAMJE) -  UDP-N-acetylbacillosamine N-acetyltransferase
Seq:
Struc:
195 a.a.
191 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.3.1.203  - UDP-N-acetylbacillosamine N-acetyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Acetyl-CoA + UDP-N-acetylbacillosamine = CoA + UDP- N,N'-diacetylbacillosamine
Acetyl-CoA
+ UDP-N-acetylbacillosamine
= CoA
+ UDP- N,N'-diacetylbacillosamine
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     protein glycosylation   2 terms 
  Biochemical function     transferase activity     3 terms  

 

 
    Added reference    
 
 
J Biol Chem 283:27937-27946 (2008)
PubMed id: 18667421  
 
 
Crystal structure and catalytic mechanism of PglD from Campylobacter jejuni.
N.B.Olivier, B.Imperiali.
 
  ABSTRACT  
 
The carbohydrate 2, 4-diacetamido-2, 4, 6-trideoxy-alpha-D-glucopyranose (BacAc(2)) is found in a variety of eubacterial pathogens. In Campylobacter jejuni, PglD acetylates the C4 amino group on UDP-2-acetamido-4-amino-2, 4, 6-trideoxy-alpha-D-glucopyranose (UDP-4-amino-sugar) to form UDP-BacAc(2). Sequence analysis predicts PglD to be a member of the left-handed beta helix family of enzymes. However, poor sequence homology between PglD and left-handed beta helix enzymes with existing structural data precludes unambiguous identification of the active site. The co-crystal structures of PglD in the presence of citrate, acetyl coenzyme A, or the UDP-4-amino-sugar were solved. The biological assembly is a trimer with one active site formed between two protomers. Residues lining the active site were identified, and results from functional assays on alanine mutants suggest His-125 is critical for catalysis, whereas His-15 and His-134 are involved in substrate binding. These results are discussed in the context of implications for proteins homologous to PglD in other pathogens.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
  20871840 R.Ristl, K.Steiner, K.Zarschler, S.Zayni, P.Messner, and C.Schäffer (2011).
The s-layer glycome-adding to the sugar coat of bacteria.
  Int J Microbiol, 2011, 0.  
20832292 H.M.Holden, P.D.Cook, and J.B.Thoden (2010).
Biosynthetic enzymes of unusual microbial sugars.
  Curr Opin Struct Biol, 20, 543-550.  
20948550 H.Nothaft, and C.M.Szymanski (2010).
Protein glycosylation in bacteria: sweeter than ever.
  Nat Rev Microbiol, 8, 765-778.  
19348502 A.Larkin, and B.Imperiali (2009).
Biosynthesis of UDP-GlcNAc(3NAc)A by WbpB, WbpE, and WbpD: enzymes in the Wbp pathway responsible for O-antigen assembly in Pseudomonas aeruginosa PAO1.
  Biochemistry, 48, 5446-5455.  
19191736 J.B.Thoden, P.D.Cook, C.Schäffer, P.Messner, and H.M.Holden (2009).
Structural and functional studies of QdtC: an N-acetyltransferase required for the biosynthesis of dTDP-3-acetamido-3,6-dideoxy-alpha-D-glucose.
  Biochemistry, 48, 2699-2709.
PDB codes: 3fs8 3fsb 3fsc
19448740 M.Demendi, and C.Creuzenet (2009).
Cj1123c (PglD), a multifaceted acetyltransferase from Campylobacter jejuni.
  Biochem Cell Biol, 87, 469-483.  
19416010 R.H.Langdon, J.Cuccui, and B.W.Wren (2009).
N-linked glycosylation in bacteria: an unexpected application.
  Future Microbiol, 4, 401-412.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.