1im5

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Crystal Structure of Pyrazinamidase of Pyrococcus horikoshii in Complex with ZincCrystal Structure of Pyrazinamidase of Pyrococcus horikoshii in Complex with Zinc

Structural highlights

1im5 is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Activity:Hydrolase, with EC number 3.5.1.19
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Bacterial pyrazinamidase (PZAase)/nicotinamidase converts pyrazinamide (PZA) to ammonia and pyrazinoic acid, which is active against Mycobacterium tuberculosis. Loss of PZAase activity is the major mechanism of pyrazinamide-resistance by M. tuberculosis. We have determined the crystal structure of the gene product of Pyrococcus horikoshii 999 (PH999), a PZAase, and its complex with zinc ion by X-ray crystallography. The overall fold of PH999 is similar to that of N-carbamoylsarcosine amidohydrolase (CSHase) of Arthrobacter sp. and YcaC of Escherichia coli, a protein with unknown physiological function. The active site of PH999 was identified by structural features that are also present in the active sites of CSHase and YcaC: a triad (D10, K94, and C133) and a cis-peptide (between V128 and A129). Surprisingly, a metal ion-binding site was revealed in the active site and subsequently confirmed by crystal structure of PH999 in complex with Zn(2+). The roles of the triad, cis-peptide, and metal ion in the catalysis are proposed. Because of extensive homology between PH999 and PZAase of M. tuberculosis (37% sequence identity), the structure of PH999 provides a structural basis for understanding PZA-resistance by M. tuberculosis harboring PZAase mutations.

Crystal structure and mechanism of catalysis of a pyrazinamidase from Pyrococcus horikoshii.,Du X, Wang W, Kim R, Yakota H, Nguyen H, Kim SH Biochemistry. 2001 Nov 27;40(47):14166-72. PMID:11714269[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Du X, Wang W, Kim R, Yakota H, Nguyen H, Kim SH. Crystal structure and mechanism of catalysis of a pyrazinamidase from Pyrococcus horikoshii. Biochemistry. 2001 Nov 27;40(47):14166-72. PMID:11714269

1im5, resolution 1.65Å

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