4C50

Crystal Structure of the Catalase-Peroxidase (KatG) D137S mutant from Mycobacterium Tuberculosis

Summary for 4C50

• Entry DOI: 10.2210/pdb4c50/pdb
• Related: 4C51
• Descriptor: CATALASE-PEROXIDASE, alpha-D-glucopyranose, PROTOPORPHYRIN IX CONTAINING FE, ... (5 entities in total)
• Functional Keywords: oxidoreductase
• Biological source: MYCOBACTERIUM TUBERCULOSIS
• Total number of polymer chains: 2
• Total formula weight: 162791.38

Authors

Hersleth, H.-P.,Zhao, X.,Magliozzo, R.S.,Andersson, K.K. (deposition date: 2013-09-10, release date: 2013-11-13, Last modification date: 2023-12-20)

Primary citation

Zhao, X.,Hersleth, H.P.,Zhu, J.,Andersson, K.K.,Magliozzo, R.S.
Access Channel Residues Ser315 and Asp137 in Mycobacterium Tuberculosis Catalase-Peroxidase (Katg) Control Peroxidatic Activation of the Pro-Drug Isoniazid.
Chem.Commun.(Camb.), 49:11650-, 2013

PubMed Abstract: Peroxidatic activation of the anti-tuberculosis pro-drug isoniazid by Mycobacterium tuberculosis catalase-peroxidase (KatG) is regulated by gating residues of a heme access channel. The steric restriction at the bottleneck of this channel is alleviated by replacement of residue Asp137 with Ser, according to crystallographic and kinetic studies.

PubMed: 24185282
DOI: 10.1039/C3CC47022A

Experimental method

X-RAY DIFFRACTION (2.5 Å)