1geb
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1geb |SIZE=350|CAPTION= <scene name='initialview01'>1geb</scene>, resolution 2.03Å | |PDB= 1geb |SIZE=350|CAPTION= <scene name='initialview01'>1geb</scene>, resolution 2.03Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CAM:CAMPHOR'>CAM</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1geb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1geb OCA], [http://www.ebi.ac.uk/pdbsum/1geb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1geb RCSB]</span> | ||
}} | }} | ||
| Line 28: | Line 31: | ||
[[Category: Park, S Y.]] | [[Category: Park, S Y.]] | ||
[[Category: Shimada, H.]] | [[Category: Shimada, H.]] | ||
| - | [[Category: CAM]] | ||
| - | [[Category: HEM]] | ||
[[Category: cytochrome p450cam]] | [[Category: cytochrome p450cam]] | ||
| - | [[Category: monooxygenase]] | + | [[Category: monooxygenase,]] |
| - | ''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 20:42:17 2008'' |
Revision as of 17:42, 30 March 2008
| |||||||
| , resolution 2.03Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Camphor 5-monooxygenase, with EC number 1.14.15.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
X-RAY CRYSTAL STRUCTURE AND CATALYTIC PROPERTIES OF THR252ILE MUTANT OF CYTOCHROME P450CAM
Overview
The structure-function relationship in cytochrome P450cam monooxygenase was studied by employing its active site mutant Thr252Ile. X-ray crystallographic analyses of the ferric d-camphor-bound form of the mutant revealed that the mutation caused a structural change in the active site giving an enlarged oxygen-binding pocket that did not contain any hydrophilic group such as the OH group of Thr and H(2)O. The enzyme showed a low monooxygenase activity of ca. 1/10 of the activity of the wild-type enzyme. Kinetic analyses of each catalytic step revealed that the rate of proton-coupled reduction of the oxygenated intermediate of the enzyme, a ternary complex of dioxygen and d-camphor with the ferrous enzyme, decreased to about 1/30 of that of the wild-type enzyme, while the rates of other catalytic steps including the reduction of the ferric d-camphor-bound form by reduced putidaredoxin did not change significantly. These results indicated that a hydrophilic group(s) such as water and/or hydroxyl group in the active site is prerequisite to a proton supply for the reduction of the oxygenated intermediate, thereby giving support for the operation of a proton transfer network composed of Thr252, Asp251, and two other amino acids and water proposed by previous investigators.
About this Structure
1GEB is a Single protein structure of sequence from Pseudomonas putida. Full crystallographic information is available from OCA.
Reference
X-ray crystal structure and catalytic properties of Thr252Ile mutant of cytochrome P450cam: roles of Thr252 and water in the active center., Hishiki T, Shimada H, Nagano S, Egawa T, Kanamori Y, Makino R, Park SY, Adachi S, Shiro Y, Ishimura Y, J Biochem. 2000 Dec;128(6):965-74. PMID:11098139
Page seeded by OCA on Sun Mar 30 20:42:17 2008
