PDBsum entry 2wjz

Lyase/transferase

PDB id: 2wjz

Contents

Protein chains

251 a.a. *

193 a.a. *

237 a.a. *

Ligands

PO4 ×3

Waters ×209

* Residue conservation analysis

PDB id:

2wjz

Name:

Lyase/transferase

Title:

Crystal structure of (hish) k181a y138a mutant of imidazoleglycerolphosphate synthase (hish hisf) which displays constitutive glutaminase activity

Structure:

Imidazole glycerol phosphate synthase hisf. Chain: a, c, e. Synonym: igp synthase cyclase subunit, igp synthase subunit hisf, imgp synthase subunit hisf, igps subunit hisf. Engineered: yes. Imidazole glycerol phosphate synthase subunit hish. Chain: b, d, f. Synonym: igp synthase glutamine amidotransferase subunit, igp synthase subunit hish, imgp synthase subunit hish, tmhish, igps

Source:

Thermotoga maritima. Organism_taxid: 2336. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expressed in: escherichia coli k-12. Expression_system_taxid: 83333.

Resolution:

2.60Å R-factor: 0.187 R-free: 0.218

Authors:

M.C.Vega,F.List,A.Razeto,M.C.Haeger,K.Babinger,J.Kuper,R.Sterner, M.Wilmanns

Key ref:

F.List et al. (2012). Catalysis uncoupling in a glutamine amidotransferase bienzyme by unblocking the glutaminase active site. Chem Biol, 19, 1589-1599. PubMed id: 23261602

Date:

02-Jun-09 Release date: 25-Aug-10

Protein chains

Q9X0C6  (HIS6_THEMA) -  Imidazole glycerol phosphate synthase subunit HisF from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)

Seq: 253 a.a.

Struc: 251 a.a.

Protein chains

Q9X0C8  (HIS5_THEMA) -  Imidazole glycerol phosphate synthase subunit HisH from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)

Seq: 201 a.a.

Struc: 193 a.a.*

Protein chain

Q9X0C6  (HIS6_THEMA) -  Imidazole glycerol phosphate synthase subunit HisF from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)

Seq: 253 a.a.

Struc: 237 a.a.

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Enzyme reactions

• Enzyme class 2: Chains A, B, C, D, E, F: E.C.4.3.2.10 - imidazole glycerol-phosphate synthase.
• Reaction: 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta- D-ribosyl)imidazole-4-carboxamide + L-glutamine = D-erythro-1-(imidazol- 4-yl)glycerol 3-phosphate + 5-amino-1-(5-phospho-beta-D- ribosyl)imidazole-4-carboxamide + L-glutamate + H⁺
• Enzyme class 3: Chains B, D, F: E.C.3.5.1.2 - glutaminase.
• Reaction: L-glutamine + H2O = L-glutamate + NH4⁺

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

Chem Biol 19:1589-1599 (2012)

PubMed id: 23261602

Catalysis uncoupling in a glutamine amidotransferase bienzyme by unblocking the glutaminase active site.

F.List, M.C.Vega, A.Razeto, M.C.Häger, R.Sterner, M.Wilmanns.

ABSTRACT

No abstract given.