PDBsum entry 3nvt

Transferase/isomerase

PDB id: 3nvt

Contents

Protein chains

345 a.a. *

327 a.a. *

Ligands

_MN ×2

ACT ×2

Waters ×763

* Residue conservation analysis

PDB id:

3nvt

Name:

Transferase/isomerase

Title:

1.95 angstrom crystal structure of a bifunctional 3-deoxy-7- phosphoheptulonate synthase/chorismate mutase (aroa) from listeria monocytogenes egd-e

Structure:

3-deoxy-d-arabino-heptulosonate 7-phosphate synthase. Chain: a, b. Engineered: yes

Source:

Listeria monocytogenes. Organism_taxid: 169963. Strain: egd-e. Gene: aroa, lmo1600. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

1.95Å R-factor: 0.156 R-free: 0.198

Authors:

A.S.Halavaty,S.H.Light,G.Minasov,L.Shuvalova,K.Kwon,W.F.Anderson, Center For Structural Genomics Of Infectious Diseases (Csgid)

Key ref:

S.H.Light et al. (2012). Structural analysis of a 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase with an N-terminal chorismate mutase-like regulatory domain. Protein Sci, 21, 887-895. PubMed id: 22505283

Date:

08-Jul-10 Release date: 28-Jul-10

Protein chain

Q8Y6T2  (Q8Y6T2_LISMO) -  3-deoxy-D-arabino-heptulosonate 7-phosphate synthase from Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)

Seq: 361 a.a.

Struc: 345 a.a.

Protein chain

Q8Y6T2  (Q8Y6T2_LISMO) -  3-deoxy-D-arabino-heptulosonate 7-phosphate synthase from Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)

Seq: 361 a.a.

Struc: 327 a.a.

Enzyme reactions

• Enzyme class 1: Chains A, B: E.C.2.5.1.54 - 3-deoxy-7-phosphoheptulonate synthase.
• Pathway: Shikimate and Chorismate Biosynthesis
• Reaction: D-erythrose 4-phosphate + phosphoenolpyruvate + H2O = 7-phospho-2- dehydro-3-deoxy-D-arabino-heptonate + phosphate

D-erythrose 4-phosphate + phosphoenolpyruvate + H2O (Bound ligand (Het Group name = ACT) matches with 40.00% similarity) = 7-phospho-2- dehydro-3-deoxy-D-arabino-heptonate + phosphate

• Enzyme class 2: Chains A, B: E.C.5.4.99.5 - chorismate mutase.

Pathway:

• Reaction: chorismate = prephenate

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

reference

Protein Sci 21:887-895 (2012)

PubMed id: 22505283

Structural analysis of a 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase with an N-terminal chorismate mutase-like regulatory domain.

S.H.Light, A.S.Halavaty, G.Minasov, L.Shuvalova, W.F.Anderson.

ABSTRACT

No abstract given.