PDBsum entry 1q1l

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protein Protein-protein interface(s) links
Lyase PDB id
Protein chains
336 a.a. *
Waters ×560
* Residue conservation analysis
PDB id:
Name: Lyase
Title: Crystal structure of chorismate synthase
Structure: Chorismate synthase. Chain: a, b, c, d. Synonym: 5-enolpyruvylshikimate-3-phosphate phospholyase. Engineered: yes
Source: Aquifex aeolicus. Organism_taxid: 63363. Gene: aroc. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Biol. unit: Tetramer (from PQS)
2.05Å     R-factor:   0.209     R-free:   0.246
Authors: C.M.Viola,V.Saridakis,D.Christendat,Midwest Center For Structural Genomics (Mcsg)
Key ref:
C.M.Viola et al. (2004). Crystal structure of chorismate synthase from Aquifex aeolicus reveals a novel beta alpha beta sandwich topology. Proteins, 54, 166-169. PubMed id: 14705034 DOI: 10.1002/prot.10592
21-Jul-03     Release date:   30-Sep-03    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
O66493  (AROC_AQUAE) -  Chorismate synthase
398 a.a.
336 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Chorismate synthase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

Shikimate and Chorismate Biosynthesis
      Reaction: 5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate
= chorismate
+ phosphate
      Cofactor: FMN
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     cellular amino acid biosynthetic process   3 terms 
  Biochemical function     lyase activity     2 terms  


DOI no: 10.1002/prot.10592 Proteins 54:166-169 (2004)
PubMed id: 14705034  
Crystal structure of chorismate synthase from Aquifex aeolicus reveals a novel beta alpha beta sandwich topology.
C.M.Viola, V.Saridakis, D.Christendat.

  Selected figure(s)  
Figure 1.
Figure 1. a: Ribbon diagram of the CS monomer. strands and helices are colored green and gold, respectively. sheet one of the - - sandwich is located on the left of the helical core and sheet two is on the right. b: Topology diagram for CS. strands ( 1- 17) and alpha helices ( 1- 10) are shown as dark gray arrows and light gray cylinders, respectively. The diagram reveals an internal 2-fold symmetry involving two equivalent major 4-stranded anti-parallel sheets and two minor 3-stranded sheets surrounding a helical core. The symmetry is disrupted by an extension in sheet two (between 8 and 10) and by a hairpin ( 13, 14). The hairpin interacts with 10. c: The tetramer of CS with each monomer colored separately. The tetramer is constructed from a dimer of dimers with AD and BC staggered by 90°. The putative binding site is located at the interface of dimers AD and BC. d: A molecular surface representation showing electrostatic potential (same orientation as part c). Acidic regions are colored red, basic regions blue and neutral regions grey. Two pockets of positive electrostatic potential (blue) on the front of the molecule represent the putative substrate binding site.
  The above figure is reprinted by permission from John Wiley & Sons, Inc.: Proteins (2004, 54, 166-169) copyright 2004.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
15502309 M.V.Dias, F.Ely, F.Canduri, J.H.Pereira, J.Frazzon, L.A.Basso, M.S.Palma, Azevedo, and D.S.Santos (2004).
Crystallization and preliminary X-ray crystallographic analysis of chorismate synthase from Mycobacterium tuberculosis.
  Acta Crystallogr D Biol Crystallogr, 60, 2003-2005.  
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