This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1smj

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1smj.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1smj.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1smj| PDB=1smj | SCENE= }}
{{STRUCTURE_1smj| PDB=1smj | SCENE= }}
-
'''Structure of the A264E mutant of cytochrome P450 BM3 complexed with palmitoleate'''
+
===Structure of the A264E mutant of cytochrome P450 BM3 complexed with palmitoleate===
-
==Overview==
+
<!--
-
The multidomain fatty-acid hydroxylase flavocytochrome P450 BM3 has been studied as a paradigm model for eukaryotic microsomal P450 enzymes because of its homology to eukaryotic family 4 P450 enzymes and its use of a eukaryotic-like diflavin reductase redox partner. High-resolution crystal structures have led to the proposal that substrate-induced conformational changes lead to removal of water as the sixth ligand to the heme iron. Concomitant changes in the heme iron spin state and heme iron reduction potential help to trigger electron transfer from the reductase and to initiate catalysis. Surprisingly, the crystal structure of the substrate-free A264E heme domain mutant reveals the enzyme to be in the conformation observed for substrate-bound wild-type P450, but with the iron in the low-spin state. This provides strong evidence that the spin-state shift observed upon substrate binding in wild-type P450 BM3 not only is caused indirectly by structural changes in the protein, but is a direct consequence of the presence of the substrate itself, similar to what has been observed for P450cam. The crystal structure of the palmitoleate-bound A264E mutant reveals that substrate binding promotes heme ligation by Glu(264), with little other difference from the palmitoleate-bound wild-type structure observable. Despite having a protein-derived sixth heme ligand in the substrate-bound form, the A264E mutant is catalytically active, providing further indication for structural rearrangement of the active site upon reduction of the heme iron, including displacement of the glutamate ligand to allow binding of dioxygen.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15020590}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15020590 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15020590}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Palmitoleate]]
[[Category: Palmitoleate]]
[[Category: Substrate binding]]
[[Category: Substrate binding]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:53:23 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:55:09 2008''

Revision as of 10:55, 29 July 2008

Image:1smj.png

Template:STRUCTURE 1smj

Structure of the A264E mutant of cytochrome P450 BM3 complexed with palmitoleate

Template:ABSTRACT PUBMED 15020590

About this Structure

1SMJ is a Single protein structure of sequence from Bacillus megaterium. Full crystallographic information is available from OCA.

Reference

A single mutation in cytochrome P450 BM3 induces the conformational rearrangement seen upon substrate binding in the wild-type enzyme., Joyce MG, Girvan HM, Munro AW, Leys D, J Biol Chem. 2004 May 28;279(22):23287-93. Epub 2004 Mar 12. PMID:15020590

Page seeded by OCA on Tue Jul 29 13:55:09 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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