2c7g

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spinqualitylabelsall models 2c7g, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

FPRA FROM MYCOBACTERIUM TUBERCULOSIS: HIS57GLN MUTANT

Overview

Mycobacterium tuberculosis FprA is a NADPH-ferredoxin reductase, functionally and structurally similar to the mammalian adrenodoxin, reductase. It is presumably involved in supplying electrons to one or more, of the pathogen's cytochrome P450s through reduced ferredoxins. It has, been proposed on the basis of crystallographic data (Bossi, R. T., et al., (2002) Biochemistry 41, 8807-8818) that the highly conserved His57 and, Glu214 whose side chains are H-bonded are involved in catalysis. Both, residues were individually changed to nonionizable amino acyl residues, through site-directed mutagenesis. Steady-state kinetics showed that the, role of Glu214 in catalysis is negligible. On the contrary, the, substitutions of His57 markedly impaired the catalytic efficiency of FprA, for ferredoxin ... [(full description)]

About this Structure

2C7G is a [Single protein] structure of sequence from [Mycobacterium tuberculosis] with NA, FAD and ODP as [ligands]. Active as [Ferredoxin--NADP(+) reductase], with EC number [1.18.1.2]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Role of the His57-Glu214 ionic couple located in the active site of Mycobacterium tuberculosis FprA., Pennati A, Razeto A, de Rosa M, Pandini V, Vanoni MA, Mattevi A, Coda A, Aliverti A, Zanetti G, Biochemistry. 2006 Jul 25;45(29):8712-20. PMID:16846214

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