We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1i19

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1i19.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1i19.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1i19| PDB=1i19 | SCENE= }}
{{STRUCTURE_1i19| PDB=1i19 | SCENE= }}
-
'''CRYSTAL STRUCTURE OF CHOLESTEROL OXIDASE FROM B.STEROLICUM'''
+
===CRYSTAL STRUCTURE OF CHOLESTEROL OXIDASE FROM B.STEROLICUM===
-
==Overview==
+
<!--
-
Cholesterol oxidase is a monomeric flavoenzyme that catalyzes the oxidation and isomerization of cholesterol to cholest-4-en-3-one. Two forms of the enzyme are known, one containing the cofactor non-covalently bound to the protein and one in which the cofactor is covalently linked to a histidine residue. The x-ray structure of the enzyme from Brevibacterium sterolicum containing covalently bound FAD has been determined and refined to 1.7-A resolution. The active site consists of a cavity sealed off from the exterior of the protein. A model for the steroid substrate, cholesterol, can be positioned in the pocket revealing the structural factors that result in different substrate binding affinities between the two known forms of the enzyme. The structure suggests that Glu(475), located at the active site cavity, may act as the base for both the oxidation and the isomerization steps of the catalytic reaction. A water-filled channel extending toward the flavin moiety, inside the substrate-binding cavity, may act as the entry point for molecular oxygen for the oxidative half-reaction. An arginine and a glutamate residue at the active site, found in two conformations are proposed to control oxygen access to the cavity from the channel. These concerted side chain movements provide an explanation for the biphasic mode of reaction with dioxygen and the ping-pong kinetic mechanism exhibited by the enzyme.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11397813}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11397813 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11397813}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Flavoenzyme]]
[[Category: Flavoenzyme]]
[[Category: Mix alpha beta]]
[[Category: Mix alpha beta]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:27:19 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 10:15:42 2008''

Revision as of 07:15, 1 July 2008

Image:1i19.png

Template:STRUCTURE 1i19

CRYSTAL STRUCTURE OF CHOLESTEROL OXIDASE FROM B.STEROLICUM

Template:ABSTRACT PUBMED 11397813

About this Structure

1I19 is a Single protein structure of sequence from Brevibacterium sterolicum. Full crystallographic information is available from OCA.

Reference

Oxygen access to the active site of cholesterol oxidase through a narrow channel is gated by an Arg-Glu pair., Coulombe R, Yue KQ, Ghisla S, Vrielink A, J Biol Chem. 2001 Aug 10;276(32):30435-41. Epub 2001 Jun 7. PMID:11397813

Page seeded by OCA on Tue Jul 1 10:15:42 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1i19"
Personal tools