1jfb: Difference between revisions

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New page: left|200px<br /><applet load="1jfb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jfb, resolution 1.0Å" /> '''X-ray structure of ni...
 
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[[Image:1jfb.jpg|left|200px]]<br /><applet load="1jfb" size="450" color="white" frame="true" align="right" spinBox="true"  
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caption="1jfb, resolution 1.0&Aring;" />
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'''X-ray structure of nitric oxide reductase (cytochrome P450nor) in the ferric resting state at atomic resolution'''<br />
'''X-ray structure of nitric oxide reductase (cytochrome P450nor) in the ferric resting state at atomic resolution'''<br />


==Overview==
==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.
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==
1JFB 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 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JFB OCA].  
1JFB 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> 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=1JFB OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Adachi, S.]]
[[Category: Adachi, S.]]
[[Category: Park, S.Y.]]
[[Category: Park, S Y.]]
[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
[[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]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:22:01 2008''

Revision as of 14:22, 21 February 2008

File:1jfb.jpg


1jfb, resolution 1.0Å

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

OverviewOverview

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 StructureAbout this Structure

1JFB 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.

ReferenceReference

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

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