1ulw

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|PDB= 1ulw |SIZE=350|CAPTION= <scene name='initialview01'>1ulw</scene>, resolution 2.00&Aring;
|PDB= 1ulw |SIZE=350|CAPTION= <scene name='initialview01'>1ulw</scene>, resolution 2.00&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene>
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|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>
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|ACTIVITY= [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]
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|ACTIVITY= <span class='plainlinks'>[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] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=[[1j3o|1J3O]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ulw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ulw OCA], [http://www.ebi.ac.uk/pdbsum/1ulw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ulw RCSB]</span>
}}
}}
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[[Category: Su, F.]]
[[Category: Su, F.]]
[[Category: Takaya, N.]]
[[Category: Takaya, N.]]
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[[Category: HEM]]
 
[[Category: cytochrome p450nor]]
[[Category: cytochrome p450nor]]
[[Category: nitric oxide reductase]]
[[Category: nitric oxide reductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:33:42 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:12:13 2008''

Revision as of 21:12, 30 March 2008


PDB ID 1ulw

Drag the structure with the mouse to rotate
, resolution 2.00Å
Ligands:
Activity: Nitric-oxide reductase, with EC number 1.7.99.7
Related: 1J3O


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal structure of P450nor Ser73Gly/Ser75Gly mutant


Overview

Nitric oxide reductase cytochrome P450nor catalyzes an unusual reaction, direct electron transfer from NAD(P)H to bound heme. Here, we succeeded in determining the crystal structure of P450nor in a complex with an NADH analogue, nicotinic acid adenine dinucleotide, which provides conclusive evidence for the mechanism of the unprecedented electron transfer. Comparison of the structure with those of dinucleotide-free forms revealed a global conformational change accompanied by intriguing local movements caused by the binding of the pyridine nucleotide. Arg64 and Arg174 fix the pyrophosphate moiety upon the dinucleotide binding. Stereo-selective hydride transfer from NADH to NO-bound heme was suggested from the structure, the nicotinic acid ring being fixed near the heme by the conserved Thr residue in the I-helix and the upward-shifted propionate side-chain of the heme. A proton channel near the NADH channel is formed upon the dinucleotide binding, which should direct continuous transfer of the hydride and proton. A salt-bridge network (Glu71-Arg64-Asp88) was shown to be crucial for a high catalytic turnover.

About this Structure

1ULW is a Single protein structure of sequence from Fusarium oxysporum. Full crystallographic information is available from OCA.

Reference

Structural evidence for direct hydride transfer from NADH to cytochrome P450nor., Oshima R, Fushinobu S, Su F, Zhang L, Takaya N, Shoun H, J Mol Biol. 2004 Sep 3;342(1):207-17. PMID:15313618

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