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.

2d0u

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2d0u.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2d0u.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2d0u| PDB=2d0u | SCENE= }}
{{STRUCTURE_2d0u| PDB=2d0u | SCENE= }}
-
'''Crystal structure of cyanide bound form of human indoleamine 2,3-dioxygenase'''
+
===Crystal structure of cyanide bound form of human indoleamine 2,3-dioxygenase===
-
==Overview==
+
<!--
-
Human indoleamine 2,3-dioxygenase (IDO) catalyzes the cleavage of the pyrrol ring of L-Trp and incorporates both atoms of a molecule of oxygen (O2). Here we report on the x-ray crystal structure of human IDO, complexed with the ligand inhibitor 4-phenylimidazole and cyanide. The overall structure of IDO shows two alpha-helical domains with the heme between them. A264 of the flexible loop in the heme distal side is in close proximity to the iron. A mutant analysis shows that none of the polar amino acid residues in the distal heme pocket are essential for activity, suggesting that, unlike the heme-containing monooxygenases (i.e., peroxidase and cytochrome P450), no protein group of IDO is essential in dioxygen activation or proton abstraction. These characteristics of the IDO structure provide support for a reaction mechanism involving the abstraction of a proton from the substrate by iron-bound dioxygen. Inactive mutants (F226A, F227A, and R231A) retain substrate-binding affinity, and an electron density map reveals that 2-(N-cyclohexylamino)ethane sulfonic acid is bound to these residues, mimicking the substrate. These findings suggest that strict shape complementarities between the indole ring of the substrate and the protein side chains are required, not for binding, but, rather, to permit the interaction between the substrate and iron-bound dioxygen in the first step of the reaction. This study provides the structural basis for a heme-containing dioxygenase mechanism, a missing piece in our understanding of heme chemistry.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16477023}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16477023 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16477023}}
==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Rsgi]]
[[Category: Rsgi]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 23:29:21 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:45:42 2008''

Revision as of 04:45, 29 July 2008

Image:2d0u.png

Template:STRUCTURE 2d0u

Crystal structure of cyanide bound form of human indoleamine 2,3-dioxygenase

Template:ABSTRACT PUBMED 16477023

About this Structure

2D0U is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of human indoleamine 2,3-dioxygenase: catalytic mechanism of O2 incorporation by a heme-containing dioxygenase., Sugimoto H, Oda S, Otsuki T, Hino T, Yoshida T, Shiro Y, Proc Natl Acad Sci U S A. 2006 Feb 21;103(8):2611-6. Epub 2006 Feb 13. PMID:16477023

Page seeded by OCA on Tue Jul 29 07:45:42 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2d0u"
Personal tools