PDBsum entry 1rf6

Transferase

PDB id: 1rf6

Contents

Protein chains

427 a.a. *

Ligands

GPJ ×4

S3P ×4

Waters ×846

* Residue conservation analysis

PDB id:

1rf6

Name:

Transferase

Title:

Structural studies of streptococcus pneumoniae epsp synthase in s3p- glp bound state

Structure:

5-enolpyruvylshikimate-3-phosphate synthase. Chain: a, b, c, d. Engineered: yes

Source:

Streptococcus pneumoniae. Organism_taxid: 1313. Gene: aroa. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.90Å R-factor: 0.218 R-free: 0.229

Authors:

H.Park,J.L.Hilsenbeck,H.J.Kim,W.A.Shuttleworth,Y.H.Park,J.N.Evans, C.Kang

Key ref:

H.Park et al. (2004). Structural studies of Streptococcus pneumoniae EPSP synthase in unliganded state, tetrahedral intermediate-bound state and S3P-GLP-bound state. Mol Microbiol, 51, 963-971. PubMed id: 14763973

Date:

07-Nov-03 Release date: 17-Feb-04

Protein chains

Q9S400  (AROA_STRPN) -  3-phosphoshikimate 1-carboxyvinyltransferase from Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)

Seq: 427 a.a.

Struc: 427 a.a.*

* PDB and UniProt seqs differ at 4 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.2.5.1.19 - 3-phosphoshikimate 1-carboxyvinyltransferase.
• Pathway: Shikimate and Chorismate Biosynthesis
• Reaction: 3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3- phosphoshikimate + phosphate

3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3- phosphoshikimate (Bound ligand (Het Group name = S3P) matches with 76.19% similarity) + phosphate

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

Mol Microbiol 51:963-971 (2004)

PubMed id: 14763973

Structural studies of Streptococcus pneumoniae EPSP synthase in unliganded state, tetrahedral intermediate-bound state and S3P-GLP-bound state.

H.Park, J.L.Hilsenbeck, H.J.Kim, W.A.Shuttleworth, Y.H.Park, J.N.Evans, C.Kang.

ABSTRACT

The shikimate pathway synthesizes aromatic amino acids and other essential metabolites that are necessary for bacteria, plants and fungi to survive. This pathway is not present in vertebrates and therefore represents an attractive target for antibacterial agents. We have successfully crystallized and solved the structure of unliganded, inhibitor-liganded and tetrahedral intermediate (TI)-liganded forms of Streptococcus pneumoniae EPSP synthase. The overall topology of the S. pneumoniae EPSP synthase is similar to that of the Escherichia coli EPSP synthase. In addition, the majority of residues responsible for ligand binding were conserved between the two proteins. TI-liganded structure provides absolute configuration of the C-2 atom from the F-PEP moiety of the enzyme-bound intermediate and also defines key residues responsible for the enzyme reaction. Comparison of the unliganded state and substrate-bound state of the enzyme provides insights into the structural mechanisms involved in dynamic events of ligand binding, domain movement and closure. This structural study of the pathogenic bacteria S. pneumoniae EPSP synthase with inhibitor and TI will provide invaluable information for the design of new-generation antibiotics.