1f25: Difference between revisions
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|PDB= 1f25 |SIZE=350|CAPTION= <scene name='initialview01'>1f25</scene>, resolution 1.4Å | |PDB= 1f25 |SIZE=350|CAPTION= <scene name='initialview01'>1f25</scene>, resolution 1.4Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NO:NITROGEN+OXIDE'>NO</scene> | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NO:NITROGEN+OXIDE'>NO</scene> | ||
|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= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1f24|1F24]], [[1f26|1F26]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1f25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f25 OCA], [http://www.ebi.ac.uk/pdbsum/1f25 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1f25 RCSB]</span> | |||
}} | }} | ||
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[[Category: Park, S Y.]] | [[Category: Park, S Y.]] | ||
[[Category: Shimizu, H.]] | [[Category: Shimizu, H.]] | ||
[[Category: cytochrome p450nor]] | [[Category: cytochrome p450nor]] | ||
[[Category: nitric oxide reductase]] | [[Category: nitric oxide reductase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:14:13 2008'' | ||
Revision as of 20:14, 30 March 2008
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| , resolution 1.4Å | |||||||
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| Ligands: | , , | ||||||
| Activity: | Nitric-oxide reductase, with EC number 1.7.99.7 | ||||||
| Related: | 1F24, 1F26
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF NO COMPLEX OF THR243ASN MUTANTS OF CYTOCHROME P450NOR
OverviewOverview
Threonine 243 of cytochrome P450nor (fungal nitric oxide reductase) corresponds to the 'conserved' Thr in the long I helix of monooxygenase cytochrome P450s. In P450nor, the replacement of Thr243 with Asn, Ala or Val makes the enzymatic activity dramatically reduce. In order to understand the roles of Thr243 in the reduction reaction of NO by P450nor, the crystal structures of three Thr243 mutants (Thr243-->Asn, Thr243-->Val, Thr243-->Ala) of P450nor were determined at a 1.4-A resolution and at cryogenic temperature. However, the hydrogen-bonding pattern in the heme pocket of these mutants is essentially similar for that of the WT enzyme. This suggests that the determination of the structure of the NADH complex of P450nor is required, in order to evaluate the role of Thr243 in its enzymatic reaction. We attempted to crystallize the NADH complex under several conditions, but have not yet been successful.
About this StructureAbout this Structure
1F25 is a Single protein structure of sequence from Fusarium oxysporum. Full crystallographic information is available from OCA.
ReferenceReference
Mutation effects of a conserved threonine (Thr243) of cytochrome P450nor on its structure and function., Obayashi E, Shimizu H, Park SY, Shoun H, Shiro Y, J Inorg Biochem. 2000 Nov;82(1-4):103-11. PMID:11132616
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