1nno
From Proteopedia
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CONFORMATIONAL CHANGES OCCURRING UPON NO BINDING IN NITRITE REDUCTASE FROM PSEUDOMONAS AERUGINOSA
Overview
Nitrite reductase (NiR) from Pseudomonas aeruginosa (EC 1.9.3.2) (NiR-Pa), is a soluble enzyme catalyzing the reduction of nitrite (NO2-) to nitric, oxide (NO). The enzyme is a 120 kDa homodimer, in which each monomer, carries one c and one d1 heme. The oxidized and reduced forms of NiR from, Paracoccus denitrificans GB17 (previously called Thiosphaera pantotropha), (NiR-Pd) have been described [Fulop, V., et al. (1995) Cell 81, 369-377;, Williams, P. A., et al. (1997) Nature 389, 406-412], and we recently, reported on the structure of oxidized NiR-Pa at 2.15 A [Nurizzo, D., et, al. (1997) Structure 5, 1157-1171]. Although the domains carrying the d1, heme are almost identical in both NiR-Pa and NiR-Pd oxidized and reduced, structures, the c heme domains show a different pattern of c ... [(full description)]
About this Structure
1NNO is a [Single protein] structure of sequence from [Pseudomonas aeruginosa] with HEC, DHE and NO as [ligands]. Active as [Transferred entry: 1.7.2.1], with EC number [1.9.3.2]. Structure known Active Sites: CSA and CSB. Full crystallographic information is available from [OCA].
Reference
Conformational changes occurring upon reduction and NO binding in nitrite reductase from Pseudomonas aeruginosa., Nurizzo D, Cutruzzola F, Arese M, Bourgeois D, Brunori M, Cambillau C, Tegoni M, Biochemistry. 1998 Oct 6;37(40):13987-96. PMID:9760233
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