1JFB

X-ray structure of nitric oxide reductase (cytochrome P450nor) in the ferric resting state at atomic resolution

Summary for 1JFB

• Entry DOI: 10.2210/pdb1jfb/pdb
• Related: 1JFC
• Descriptor: nitric-oxide reductase cytochrome P450 55A1, PROTOPORPHYRIN IX CONTAINING FE, GLYCEROL, ... (4 entities in total)
• Functional Keywords: nitric oxide reductase, cytochrome p450nor, atomic resolution, riken structural genomics/proteomics initiative, rsgi, structural genomics, oxidoreductase
• Biological source: Fusarium oxysporum
• Total number of polymer chains: 1
• Total formula weight: 45230.37

Authors

Shimizu, H.,Adachi, S.,Park, S.Y.,Shiro, Y.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2001-06-20, release date: 2001-12-20, Last modification date: 2024-03-13)

Primary citation

Shimizu, H.,Park, S.Y.,Shiro, Y.,Adachi, S.
X-ray structure of nitric oxide reductase (cytochrome P450nor) at atomic resolution.
Acta Crystallogr.,Sect.D, 58:81-89, 2002

PubMed Abstract: Crystal structures of the nitric oxide reductase cytochrome P450nor (P450nor) in the ferric resting and the ferrous carbonmonoxy (CO) states have been determined at 1.00 and 1.05 A resolution, respectively. P450nor consists of 403 amino-acid residues (46 kDa) and is one of the largest proteins refined to this resolution so far. The final models have conventional R factors of 10.2% (ferric resting) and 11.7% (ferrous CO), with mean coordinate errors of 0.028 (ferric resting) and 0.030 A (ferrous CO) as calculated from inversion of the full positional least-squares matrix. Owing to the atomic resolution, novel features are found in the refined structures. Firstly, two orientations of the haem are observed both in the ferric resting and the ferrous CO states. Secondly, a disordered water molecule bound to the haem iron is found in the ferric resting state. In addition, the accurate structures at atomic resolution enabled the examination of general stereochemical parameters that are commonly used in refinement cycles of protein structures.

PubMed: 11752781
DOI: 10.1107/S0907444901017383

Experimental method

X-RAY DIFFRACTION (1 Å)