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PDBsum entry 2rl1

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protein ligands links
Transferase PDB id
2rl1
Jmol
Contents
Protein chain
420 a.a. *
Ligands
SO4
UD1
Waters ×346
* Residue conservation analysis
PDB id:
2rl1
Name: Transferase
Title: Crystal structure of udp-n-acetylglucosamine enolpyruvyl transferase from haemophilus influenzae in complex with udp-n-acetylglucosamine
Structure: Udp-n-acetylglucosamine 1- carboxyvinyltransferase. Chain: a. Synonym: enoylpyruvate transferase, udp-n- acetylglucosamine enolpyruvyl transferase, ept. Engineered: yes
Source: Haemophilus influenzae. Organism_taxid: 727. Gene: murz. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.20Å     R-factor:   0.199     R-free:   0.248
Authors: H.J.Yoon,S.W.Suh
Key ref:
H.J.Yoon et al. (2008). Crystal structure of UDP-N-acetylglucosamine enolpyruvyl transferase from Haemophilus influenzae in complex with UDP-N-acetylglucosamine and fosfomycin. Proteins, 71, 1032-1037. PubMed id: 18247346 DOI: 10.1002/prot.21959
Date:
18-Oct-07     Release date:   25-Mar-08    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P45025  (MURA_HAEIN) -  UDP-N-acetylglucosamine 1-carboxyvinyltransferase
Seq:
Struc:
424 a.a.
420 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.5.1.7  - UDP-N-acetylglucosamine 1-carboxyvinyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Peptidoglycan Biosynthesis (Part 1)
      Reaction: Phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP- N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
Phosphoenolpyruvate
+ UDP-N-acetyl-alpha-D-glucosamine
Bound ligand (Het Group name = UD1)
corresponds exactly
= phosphate
+ UDP- N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
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     cell cycle   5 terms 
  Biochemical function     catalytic activity     4 terms  

 

 
    Added reference    
 
 
DOI no: 10.1002/prot.21959 Proteins 71:1032-1037 (2008)
PubMed id: 18247346  
 
 
Crystal structure of UDP-N-acetylglucosamine enolpyruvyl transferase from Haemophilus influenzae in complex with UDP-N-acetylglucosamine and fosfomycin.
H.J.Yoon, S.J.Lee, B.Mikami, H.J.Park, J.Yoo, S.W.Suh.
 
  ABSTRACT  
 
No abstract given.

 
  Selected figure(s)  
 
Figure 1.
Figure 1. Ligand electron density and structural comparisons. (A) Electron density of UDP-N-acetylglucosamine (UDP-NAG) (colored in orange, left panel) and fosfomycin (colored in blue, right panel) bound in the active site of the ternary complex of H. influenzae MurA. The 2Fo - Fc map, contoured at 1.0 , is superimposed on the refined model. Fosfomycin covalently bound to Cys117 and UDP-N-acetylglucosamine are shown in stick models. (B) Stereo ribbon diagram of superimposed structures of the H. influenzae MurA binary complex (colored in gray) and ternary complex (colored in blue). (C) Stereo ribbon diagram of superimposed MurA structures with a half-open conformation of the active site loop. The loop adopts similar half-open conformations in H. influenzae MurA (blue) complexed with UDP-N-acetylglucosamine and fosfomycin, E. coli MurA (magenta) complexed with a tetrahedral reaction intermediate (1A2N),[14] and E. cloacae MurA (cyan) complexed with a reaction product (1RYW).[15] UDP-N-acetylglucosamine (orange) and fosfomycin (blue) bound to H. influenzae MurA are shown in stick models. (D) Stereo ribbon diagram of superimposed MurA structures with different conformations of the active site loop. The loop takes a closed conformation in E. coli MurA (green) complexed with UDP-N-acetylglucosamine and fosfomycin (1UAE).[10] It adopts a half-open conformation in H. influenzae MurA (blue) complexed with UDP-N-acetylglucosamine and fosfomycin. It has an open conformation in the unliganded E. cloacae MurA (pink) (1NAW).[9] UDP-N-acetylglucosamine (orange) and fosfomycin (blue) bound to H. influenzae MurA, as well as fosfomycin bound to E. coli MurA (green), are shown in stick models.
Figure 2.
Figure 2. Alignment of MurA sequences. The residue numbers are for MurA from H. influenzae. HI is for MurA from H. influenzae (SWISS-PROT entry P45025), EC for E. coli (P0A749), EC2 for E. cloacae (P33038), HP for Helicobacter pylori (P56189), MT for Mycobacterium tuberculosis (P0A5L2), BS for Bacillus subtilis (P19670), and SA for Staphylococcus aureus (P65456). Strictly conserved residues and semiconserved residues are colored in pink and yellow, respectively. The inhibitor fosfomycin binds covalently to a cysteine of the active site loop (indicated by a deep blue box). Two residue insertions in a variable loop between strands 4 and 5 are also indicated by a light blue box. The secondary structures of H. influenzae MurA are indicated above the sequences. This figure was drawn with ClustalX[16] and GeneDoc (http://www.nrbsc.org/downloads/).
 
  The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2008, 71, 1032-1037) copyright 2008.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20392080 H.Han, Y.Yang, S.H.Olesen, A.Becker, S.Betzi, and E.Schönbrunn (2010).
The fungal product terreic acid is a covalent inhibitor of the bacterial cell wall biosynthetic enzyme UDP-N-acetylglucosamine 1-carboxyvinyltransferase (MurA) .
  Biochemistry, 49, 4276-4282.
PDB codes: 3kqa 3kqj 3kr6 3lth
19892831 S.Homi, K.Takechi, K.Tanidokoro, H.Sato, S.Takio, and H.Takano (2009).
The peptidoglycan biosynthesis genes MurA and MraY are related to chloroplast division in the moss Physcomitrella patens.
  Plant Cell Physiol, 50, 2047-2056.  
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.