4AIV

Crystal Structure of putative NADH-dependent nitrite reductase small subunit from Mycobacterium tuberculosis

Summary for 4AIV

Entry DOI	10.2210/pdb4aiv/pdb
Descriptor	PROBABLE NITRITE REDUCTASE [NAD(P)H] SMALL SUBUNIT NIRD, GLYCEROL (3 entities in total)
Functional Keywords	oxidoreductase, nitrite metabolism
Biological source	MYCOBACTERIUM TUBERCULOSIS
Total number of polymer chains	1
Total formula weight	12591.31
Authors	Izumi, A.,Schnell, R.,Schneider, G. (deposition date: 2012-02-15, release date: 2012-09-12, Last modification date: 2023-12-20)
Primary citation	Izumi, A.,Schnell, R.,Schneider, G. Crystal Structure of Nird, the Small Subunit of the Nitrite Reductase Nirbd from Mycobacterium Tuberculosis, at 2.0 Angstrom Resolution Proteins, 80:2799-, 2012 Cited by PubMed Abstract: NirD is part of the nitrite reductase complex NirBD that catalyses the reduction of nitrite to NH(3) 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. PubMed: 22965870 DOI: 10.1002/PROT.24177 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2 Å)

Structure validation