1vgi: Difference between revisions
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|PDB= 1vgi |SIZE=350|CAPTION= <scene name='initialview01'>1vgi</scene>, resolution 1.9Å | |PDB= 1vgi |SIZE=350|CAPTION= <scene name='initialview01'>1vgi</scene>, resolution 1.9Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=XE:XENON'>XE</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Heme_oxygenase Heme oxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.3 1.14.99.3] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Heme_oxygenase Heme oxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.3 1.14.99.3] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1ulx|1ULX]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vgi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vgi OCA], [http://www.ebi.ac.uk/pdbsum/1vgi PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1vgi RCSB]</span> | |||
}} | }} | ||
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[[Category: Sakamoto, H.]] | [[Category: Sakamoto, H.]] | ||
[[Category: Sugishima, M.]] | [[Category: Sugishima, M.]] | ||
[[Category: hydrophobic cavity]] | [[Category: hydrophobic cavity]] | ||
[[Category: xenon binding]] | [[Category: xenon binding]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:24:06 2008'' | ||
Revision as of 00:24, 31 March 2008
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| , resolution 1.9Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Activity: | Heme oxygenase, with EC number 1.14.99.3 | ||||||
| Related: | 1ULX
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of xenon bound rat heme-heme oxygenase-1 complex
OverviewOverview
Heme oxygenase (HO) catalyzes physiological heme degradation using O(2) and reducing equivalents to produce biliverdin, iron, and CO. Notably, the HO reaction proceeds without product inhibition by CO, which is generated in the conversion reaction of alpha-hydroxyheme to verdoheme, although CO is known to be a potent inhibitor of HO and other heme proteins. In order to probe how endogenous CO is released from the reaction site, we collected X-ray diffraction data from a crystal of the CO-bound form of the ferrous heme-HO complex in the dark and under illumination by a red laser at approximately 35 K. The difference Fourier map indicates that the CO ligand is partially photodissociated from the heme and that the photolyzed CO is trapped in a hydrophobic cavity adjacent to the heme pocket. This hydrophobic cavity was occupied also by xenon, which is similar to CO in terms of size and properties. Taking account of the affinity of CO for the ferrous verdoheme-HO complex being much weaker than that for the ferrous heme complex, the CO derived from alpha-hydroxyheme would be trapped preferentially in the hydrophobic cavity but not coordinated to the iron of verdoheme. This structural device would ensure the smooth progression of the subsequent reaction, from verdoheme to biliverdin, which requires O(2) binding to verdoheme.
About this StructureAbout this Structure
1VGI is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
ReferenceReference
CO-trapping site in heme oxygenase revealed by photolysis of its co-bound heme complex: mechanism of escaping from product inhibition., Sugishima M, Sakamoto H, Noguchi M, Fukuyama K, J Mol Biol. 2004 Jul 30;341(1):7-13. PMID:15312758
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