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Transferase PDB id
2oi5
Jmol
Contents
Protein chains
449 a.a. *
Ligands
SO4 ×3
ACO ×2
UD1 ×2
Metals
_MG ×5
Waters ×629
* Residue conservation analysis
PDB id:
2oi5
Name: Transferase
Title: E. Coli glmu- complex with udp-glcnac and acetyl-coa
Structure: Bifunctional protein glmu. Chain: a, b. Engineered: yes
Source: Escherichia coli. Organism_taxid: 562. Gene: glmu. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Resolution:
2.25Å     R-factor:   0.176     R-free:   0.219
Authors: L.R.Olsen,M.W.Vetting,S.L.Roderick
Key ref:
L.R.Olsen et al. (2007). Structure of the E. coli bifunctional GlmU acetyltransferase active site with substrates and products. Protein Sci, 16, 1230-1235. PubMed id: 17473010 DOI: 10.1110/ps.072779707
Date:
10-Jan-07     Release date:   19-Jun-07    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P0ACC7  (GLMU_ECOLI) -  Bifunctional protein GlmU
Seq:
Struc: 		456 a.a.
449 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class 1: E.C.2.3.1.157  - Glucosamine-1-phosphate N-acetyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway: 		UDP-N-acetylglucosamine Biosynthesis
      Reaction: Acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D- glucosamine 1-phosphate
Acetyl-CoA
Bound ligand (Het Group name = ACO)
corresponds exactly 		+ alpha-D-glucosamine 1-phosphate
 = CoA
 +
N-acetyl-alpha-D- glucosamine 1-phosphate
Bound ligand (Het Group name = UD1)
matches with 48.00% similarity
   Enzyme class 2: E.C.2.7.7.23  - UDP-N-acetylglucosamine diphosphorylase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
      Reaction: UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N- acetyl-D-glucosamine
UTP
 + N-acetyl-alpha-D-glucosamine 1-phosphate
 = diphosphate
 +
UDP-N- acetyl-D-glucosamine
Bound ligand (Het Group name = UD1)
corresponds exactly
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     metabolic process   8 terms 
  Biochemical function     catalytic activity     10 terms  

 

 
    reference    
 
 
DOI no: 10.1110/ps.072779707 Protein Sci 16:1230-1235 (2007)
PubMed id: 17473010  
 
 
Structure of the E. coli bifunctional GlmU acetyltransferase active site with substrates and products.
L.R.Olsen, M.W.Vetting, S.L.Roderick.
 
  ABSTRACT  
 
The biosynthesis of UDP-GlcNAc in bacteria is carried out by GlmU, an essential bifunctional uridyltransferase that catalyzes the CoA-dependent acetylation of GlcN-1-PO(4) to form GlcNAc-1-PO(4) and its subsequent condensation with UTP to form pyrophosphate and UDP-GlcNAc. As a metabolite, UDP-GlcNAc is situated at a branch point leading to the biosynthesis of lipopolysaccharide and peptidoglycan. Consequently, GlmU is regarded as an important target for potential antibacterial agents. The crystal structure of the Escherichia coli GlmU acetyltransferase active site has been determined in complexes with acetyl-CoA, CoA/GlcN-1-PO(4), and desulpho-CoA/GlcNAc-1-PO(4). These structures reveal the enzyme groups responsible for binding the substrates. A superposition of these complex structures suggests that the 2-amino group of GlcN-1-PO(4) is positioned in proximity to the acetyl-CoA to facilitate direct attack on its thioester by a ternary complex mechanism.
 
  Selected figure(s)  
 
Figure 1.
Figure 1. E. coli GlmU in complex with substrates. (A) Native trimeric structure of GlmU. The three acetyltransferase active sites
 
  The above figure is reprinted by permission from the Protein Society: Protein Sci (2007, 16, 1230-1235) copyright 2007.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21370307 J.F.Trempe, S.Shenker, G.Kozlov, and K.Gehring (2011).
Self-association studies of the bifunctional N-acetylglucosamine-1-phosphate uridyltransferase from Escherichia coli.
  Protein Sci, 20, 745-752.  
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.  
19448740 M.Demendi, and C.Creuzenet (2009).
Cj1123c (PglD), a multifaceted acetyltransferase from Campylobacter jejuni.
  Biochem Cell Biol, 87, 469-483.  
19349513 M.P.Pereira, J.E.Blanchard, C.Murphy, S.L.Roderick, and E.D.Brown (2009).
High-throughput screening identifies novel inhibitors of the acetyltransferase activity of Escherichia coli GlmU.
  Antimicrob Agents Chemother, 53, 2306-2311.  
19237750 Z.Zhang, E.M.Bulloch, R.D.Bunker, E.N.Baker, and C.J.Squire (2009).
Structure and function of GlmU from Mycobacterium tuberculosis.
  Acta Crystallogr D Biol Crystallogr, 65, 275-283.
PDB codes: 2qkx 3d8v 3d98
18266853 H.Barreteau, A.Kovac, A.Boniface, M.Sova, S.Gobec, and D.Blanot (2008).
Cytoplasmic steps of peptidoglycan biosynthesis.
  FEMS Microbiol Rev, 32, 168-207.  
18218712 I.Mochalkin, S.Lightle, L.Narasimhan, D.Bornemeier, M.Melnick, S.Vanderroest, and L.McDowell (2008).
Structure of a small-molecule inhibitor complexed with GlmU from Haemophilus influenzae reveals an allosteric binding site.
  Protein Sci, 17, 577-582.
PDB code: 2vd4
18667421 N.B.Olivier, and B.Imperiali (2008).
Crystal structure and catalytic mechanism of PglD from Campylobacter jejuni.
  J Biol Chem, 283, 27937-27946.
PDB codes: 3bss 3bsw 3bsy
18573680 W.Zhang, V.C.Jones, M.S.Scherman, S.Mahapatra, D.Crick, S.Bhamidi, Y.Xin, M.R.McNeil, and Y.Ma (2008).
Expression, essentiality, and a microtiter plate assay for mycobacterial GlmU, the bifunctional glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase.
  Int J Biochem Cell Biol, 40, 2560-2571.  
18029420 I.Mochalkin, S.Lightle, Y.Zhu, J.F.Ohren, C.Spessard, N.Y.Chirgadze, C.Banotai, M.Melnick, and L.McDowell (2007).
Characterization of substrate binding and catalysis in the potential antibacterial target N-acetylglucosamine-1-phosphate uridyltransferase (GlmU).
  Protein Sci, 16, 2657-2666.
PDB codes: 2v0h 2v0i 2v0j 2v0k 2v0l
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.