2qbl: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
|PDB= 2qbl |SIZE=350|CAPTION= <scene name='initialview01'>2qbl</scene>, resolution 1.800Å | |PDB= 2qbl |SIZE=350|CAPTION= <scene name='initialview01'>2qbl</scene>, resolution 1.800Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=CAM:CAMPHOR'>CAM</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Camphor_5-monooxygenase Camphor 5-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.15.1 1.14.15.1] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Camphor_5-monooxygenase Camphor 5-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.15.1 1.14.15.1] </span> | ||
|GENE= camC, cyp101 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=303 Pseudomonas putida]) | |GENE= camC, cyp101 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=303 Pseudomonas putida]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[2qbm|2QBM]], [[2qbn|2QBN]], [[2qbo|2QBO]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qbl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qbl OCA], [http://www.ebi.ac.uk/pdbsum/2qbl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2qbl RCSB]</span> | |||
}} | }} | ||
| Line 27: | Line 30: | ||
[[Category: Schlichting, I.]] | [[Category: Schlichting, I.]] | ||
[[Category: Sligar, S D.]] | [[Category: Sligar, S D.]] | ||
[[Category: conserved active site residue]] | [[Category: conserved active site residue]] | ||
[[Category: cyp101]] | [[Category: cyp101,mutant]] | ||
[[Category: gly248]] | [[Category: gly248]] | ||
[[Category: heme geometry]] | [[Category: heme geometry]] | ||
[[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 Mon Mar 31 04:47:21 2008'' | ||
Revision as of 04:47, 31 March 2008
| |||||||
| , resolution 1.800Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | camC, cyp101 (Pseudomonas putida) | ||||||
| Activity: | Camphor 5-monooxygenase, with EC number 1.14.15.1 | ||||||
| Related: | 2QBM, 2QBN, 2QBO
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of ferric G248T cytochrome P450cam
OverviewOverview
Distal pocket water molecules have been widely implicated in the delivery of protons required in O-O bond heterolysis in the P450 reaction cycle. Targeted dehydration of the cytochrome P450cam (CYP101) distal pocket through mutagenesis of a distal pocket glycine to either valine or threonine results in the alteration of spin state equilibria, and has dramatic consequences on the catalytic rate, coupling efficiency, and kinetic solvent isotope effect parameters, highlighting an important role of the active-site hydration level on P450 catalysis. Cryoradiolysis of the mutant CYP101 oxyferrous complexes further indicates a specific perturbation of proton-transfer events required for the transformation of ferric-peroxo to ferric-hydroperoxo states. Finally, crystallography of the 248Val and 248Thr mutants in both the ferric camphor bound resting state and ferric-cyano adducts shows both the alteration of hydrogen-bonding networks and the alteration of heme geometry parameters. Taken together, these results indicate that the distal pocket microenvironment governs the transformation of reactive heme-oxygen intermediates in P450 cytochromes.
About this StructureAbout this Structure
2QBL is a Single protein structure of sequence from Pseudomonas putida. Full crystallographic information is available from OCA.
ReferenceReference
Alteration of P450 distal pocket solvent leads to impaired proton delivery and changes in heme geometry., Makris TM, von Koenig K, Schlichting I, Sligar SG, Biochemistry. 2007 Dec 11;46(49):14129-40. Epub 2007 Nov 15. PMID:18001135
Page seeded by OCA on Mon Mar 31 04:47:21 2008