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Crystal structure of NirD, the small subunit of the nitrite reductase NirbD from Mycobacterium tuberculosis at 2.0 Å resolution
Author(s) -
Izumi Atsushi,
Schnell Robert,
Schneider Gunter
Publication year - 2012
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.24177
Subject(s) - mycobacterium tuberculosis , nitrite reductase , resolution (logic) , protein subunit , nitrite , tuberculosis , crystal structure , crystal (programming language) , nitrate reductase , chemistry , reductase , microbiology and biotechnology , crystallography , biology , biochemistry , medicine , enzyme , nitrate , pathology , computer science , organic chemistry , gene , programming language , artificial intelligence
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. Proteins 2012. © 2012 Wiley Periodicals, Inc.