Database accession: MF7000162
Name: Isochorismate-pyruvate lyase (Pseudomonas aeruginosa)
PDB ID: 2h9c
Experimental method: X-ray (2.35 Å)
Assembly: Homodimer
Source organism: Pseudomonas aeruginosa
Primary publication of the structure:
Zaitseva J, Lu J, Olechoski KL, Lamb AL
Two crystal structures of the isochorismate pyruvate lyase from Pseudomonas aeruginosa.
(2006) J. Biol. Chem. 281: 33441-9
PMID: 16914555
Abstract:
Enzymatic systems that exploit pericyclic reaction mechanisms are rare. A recent addition to this class is the enzyme PchB, an 11.4-kDa isochorismate pyruvate lyase from Pseudomonas aeruginosa. The apo and pyruvate-bound structures of PchB reveal that the enzyme is a structural homologue of chorismate mutases in the AroQalpha class despite low sequence identity (20%). The enzyme is an intertwined dimer of three helices with connecting loops, and amino acids from each monomer participate in each of two active sites. The apo structure (2.35 A resolution) has one dimer per asymmetric unit with nitrate bound in an open active site. The loop between the first and second helices is disordered, providing a gateway for substrate entry and product exit. The pyruvate-bound structure (1.95 A resolution) has two dimers per asymmetric unit. One has two open active sites like the apo structure, and the other has two closed active sites with the loop between the first and second helices ordered for catalysis. Determining the structure of PchB is part of a larger effort to elucidate protein structures involved in siderophore biosynthesis, as these enzymes are crucial for bacterial iron uptake and virulence and have been identified as antimicrobial drug targets.
Annotations from the GeneOntology database. Only terms that fit at least two of the interacting proteins are shown. Molecular function:
carbon-oxygen lyase activity carbon-oxygen lyase activity
chorismate mutase activity chorismate mutase activity
isochorismate pyruvate lyase activity isochorismate pyruvate lyase activity
Biological process:
chorismate metabolic process chorismate metabolic process
pyochelin biosynthetic process pyochelin biosynthetic process
salicylic acid biosynthetic process salicylic acid biosynthetic process
Cellular component: not assigned
Structural annotations of the participating protein chains.Entry contents: 2 distinct polypeptide molecules
Chains: A, B
Notes: All chains according to the most probable oligomerization state stored in PDBe were considered.
Number of unique protein segments: 1
Name: Isochorismate pyruvate lyase
Source organism: Pseudomonas aeruginosa
Length: 101 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMKTPEDCTGLADIREAIDRIDLDIVQALGRRMDYVKAASRFKASEAAIPAPERVAAMLPERARWAEENGLDAPFVEGLFAQIIHWYIAEQIKYWRQTRGAA
UniProtKB AC: Q51507 (positions: 1-96)
Coverage: 95%
Name: Isochorismate pyruvate lyase
Source organism: Pseudomonas aeruginosa
Length: 101 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMKTPEDCTGLADIREAIDRIDLDIVQALGRRMDYVKAASRFKASEAAIPAPERVAAMLPERARWAEENGLDAPFVEGLFAQIIHWYIAEQIKYWRQTRGAA
UniProtKB AC: Q51507 (positions: 1-92)
Coverage: 91%
Evidence demonstrating that the participating proteins are unstructured prior to the interaction and their folding is coupled to binding. Representative domain in related structures: Chorismate mutase type II
Evidence level: Indirect evidence
Evidence coverage: The full structure participates in mutual synergistic folding.
Complex Evidence:
The enzyme is an intertwined dimer of three helices with connecting loops. The N-terminal helices of the two monomers twine together to form an anti-parallel coiled-coil with a hydrophobic interaction surface. The loop between the first and second helices is disordered (PMID:16914555).
Chain A:
N/A
Chain B:
N/A
Surface and contacts features:
Structures from the PDB that contain the same number of proteins, and the proteins from the two structures show a sufficient degree of pairwise similarity, i.e. they belong to the same UniRef90 cluster (the full proteins exhibit at least 90% sequence identity) and convey roughly the same region to their respective interactions (the two regions from the two proteins share a minimum of 70% overlap). Download the CIF file (.cif)
Download this entry's XML file (.xml)
Download this entry's JSON file (.json)
