1jfc
From Proteopedia
(New page: 200px<br /><applet load="1jfc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jfc, resolution 1.05Å" /> '''X-ray structure of n...) |
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| - | [[Image:1jfc.jpg|left|200px]]<br /><applet load="1jfc" size=" | + | [[Image:1jfc.jpg|left|200px]]<br /><applet load="1jfc" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1jfc, resolution 1.05Å" /> | caption="1jfc, resolution 1.05Å" /> | ||
'''X-ray structure of nitric oxide reductase (cytochrome P450nor) in the ferrous CO state at atomic resolution'''<br /> | '''X-ray structure of nitric oxide reductase (cytochrome P450nor) in the ferrous CO state at atomic resolution'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Crystal structures of the nitric oxide reductase cytochrome P450nor | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1JFC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Fusarium_oxysporum Fusarium oxysporum] with HEM, CMO and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Nitric-oxide_reductase Nitric-oxide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.99.7 1.7.99.7] Full crystallographic information is available from [http:// | + | 1JFC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Fusarium_oxysporum Fusarium oxysporum] with <scene name='pdbligand=HEM:'>HEM</scene>, <scene name='pdbligand=CMO:'>CMO</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Nitric-oxide_reductase Nitric-oxide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.99.7 1.7.99.7] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JFC OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Adachi, S.]] | [[Category: Adachi, S.]] | ||
| - | [[Category: Park, S | + | [[Category: Park, S Y.]] |
| - | [[Category: RSGI, RIKEN | + | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] |
[[Category: Shimizu, H.]] | [[Category: Shimizu, H.]] | ||
[[Category: Shiro, Y.]] | [[Category: Shiro, Y.]] | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:22:02 2008'' |
Revision as of 11:22, 21 February 2008
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X-ray structure of nitric oxide reductase (cytochrome P450nor) in the ferrous CO state at atomic resolution
Overview
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.
About this Structure
1JFC is a Single protein structure of sequence from Fusarium oxysporum with , and as ligands. Active as Nitric-oxide reductase, with EC number 1.7.99.7 Full crystallographic information is available from OCA.
Reference
X-ray structure of nitric oxide reductase (cytochrome P450nor) at atomic resolution., Shimizu H, Park SY, Shiro Y, Adachi S, Acta Crystallogr D Biol Crystallogr. 2002 Jan;58(Pt 1):81-9. Epub 2001 Dec, 21. PMID:11752781
Page seeded by OCA on Thu Feb 21 13:22:02 2008
Categories: Fusarium oxysporum | Nitric-oxide reductase | Single protein | Adachi, S. | Park, S Y. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Shimizu, H. | Shiro, Y. | CMO | GOL | HEM | Atomic resolution | Carbon monoxide | Cytochrome p450nor | Nitric oxide reductase | Riken structural genomics/proteomics initiative | Rsgi | Structural genomics
