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Structure Note
Crystal structure of NirD, the small subunit of the nitrite reductase NirbD from Mycobacterium tuberculosis at 2.0 Å resolution
Article first published online: 29 SEP 2012
DOI: 10.1002/prot.24177
Copyright © 2012 Wiley Periodicals, Inc.
Issue
Proteins: Structure, Function, and Bioinformatics
Volume 80, Issue 12, pages 2799–2803, December 2012
Additional Information
How to Cite
Izumi, A., Schnell, R. and Schneider, G. (2012), Crystal structure of NirD, the small subunit of the nitrite reductase NirbD from Mycobacterium tuberculosis at 2.0 Å resolution. Proteins, 80: 2799–2803. doi: 10.1002/prot.24177
Publication History
- Issue published online: 1 NOV 2012
- Article first published online: 29 SEP 2012
- Accepted manuscript online: 10 SEP 2012 06:59AM EST
- Manuscript Accepted: 26 AUG 2012
- Manuscript Revised: 1 AUG 2012
- Manuscript Received: 25 JUN 2012
Funded by
- Swedish Governmental Agency for Innovation Systems (VINNOVA)
- Abstract
- Article
- References
- Cited By
Keywords:
- nitrite reductase;
- NirB;
- NirD;
- electron transfer;
- Rieske [Fe2-S2] cluster;
- anaerobic respiration;
- Mycobacterium tuberculosis
Abstract
NirD is part of the nitrite reductase complex NirBD that catalyses the reduction of nitrite to NH3 in nitrate assimilation and anaerobic respiration. The crystal structure analysis of NirD from Mycobacterium tuberculosis shows a double β-sandwich fold. NirD is related in three-dimensional structure and sequence to the Rieske proteins; however, it does not contain any Fe–S cluster or other cofactors that might be involved in electron transfer. A cysteine residue at the protein surface, conserved in NirD homologues lacking the iron–sulfur cluster might be important for the interaction with NirB and possibly stabilize one of the Fe–S centers in this subunit. Proteins 2012. © 2012 Wiley Periodicals, Inc.