1po5: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
|PDB= 1po5 |SIZE=350|CAPTION= <scene name='initialview01'>1po5</scene>, resolution 1.6Å | |PDB= 1po5 |SIZE=350|CAPTION= <scene name='initialview01'>1po5</scene>, resolution 1.6Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene> | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Unspecific_monooxygenase Unspecific monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.14.1 1.14.14.1] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Unspecific_monooxygenase Unspecific monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.14.1 1.14.14.1] </span> | ||
|GENE= 2B4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9986 Oryctolagus cuniculus]) | |GENE= 2B4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9986 Oryctolagus cuniculus]) | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1po5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1po5 OCA], [http://www.ebi.ac.uk/pdbsum/1po5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1po5 RCSB]</span> | |||
}} | }} | ||
| Line 31: | Line 34: | ||
[[Category: Wester, M R.]] | [[Category: Wester, M R.]] | ||
[[Category: White, M A.]] | [[Category: White, M A.]] | ||
[[Category: cyp 2b4]] | [[Category: cyp 2b4]] | ||
[[Category: cyp lm2]] | [[Category: cyp lm2]] | ||
| Line 39: | Line 41: | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
''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 23:02:16 2008'' | ||
Revision as of 23:02, 30 March 2008
| |||||||
| , resolution 1.6Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | 2B4 (Oryctolagus cuniculus) | ||||||
| Activity: | Unspecific monooxygenase, with EC number 1.14.14.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of mammalian cytochrome P450 2B4
OverviewOverview
The xenobiotic metabolizing cytochromes P450 (P450s) are among the most versatile biological catalysts known, but knowledge of the structural basis for their broad substrate specificity has been limited. P450 2B4 has been frequently used as an experimental model for biochemical and biophysical studies of these membrane proteins. A 1.6-A crystal structure of P450 2B4 reveals a large open cleft that extends from the protein surface directly to the heme iron between the alpha-helical and beta-sheet domains without perturbing the overall P450 fold. This cleft is primarily formed by helices B' to C and F to G. The conformation of these regions is dramatically different from that of the other structurally defined mammalian P450, 2C5/3LVdH, in which the F to G and B' to C regions encapsulate one side of the active site to produce a closed form of the enzyme. The open conformation of 2B4 is trapped by reversible formation of a homodimer in which the residues between helices F and G of one molecule partially fill the open cleft of a symmetry-related molecule, and an intermolecular coordinate bond occurs between H226 and the heme iron. This dimer is observed both in solution and in the crystal. Differences between the structures of 2C5 and 2B4 suggest that defined regions of xenobiotic metabolizing P450s may adopt a substantial range of energetically accessible conformations without perturbing the overall fold. This conformational flexibility is likely to facilitate substrate access, metabolic versatility, and product egress.
About this StructureAbout this Structure
1PO5 is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.
ReferenceReference
An open conformation of mammalian cytochrome P450 2B4 at 1.6-A resolution., Scott EE, He YA, Wester MR, White MA, Chin CC, Halpert JR, Johnson EF, Stout CD, Proc Natl Acad Sci U S A. 2003 Nov 11;100(23):13196-201. Epub 2003 Oct 16. PMID:14563924
Page seeded by OCA on Sun Mar 30 23:02:16 2008