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.


2rgz

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2rgz.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2rgz.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2rgz| PDB=2rgz | SCENE= }}
{{STRUCTURE_2rgz| PDB=2rgz | SCENE= }}
-
'''Ensemble refinement of the protein crystal structure of human heme oxygenase-2 C127A (HO-2) with bound heme'''
+
===Ensemble refinement of the protein crystal structure of human heme oxygenase-2 C127A (HO-2) with bound heme===
-
==Overview==
+
<!--
-
Heme oxygenase (HO) catalyzes the first step in the heme degradation pathway. The crystal structures of apo- and heme-bound truncated human HO-2 reveal a primarily alpha-helical architecture similar to that of human HO-1 and other known HOs. Proper orientation of heme in HO-2 is required for the regioselective oxidation of the alpha-mesocarbon. This is accomplished by interactions within the heme binding pocket, which is made up of two helices. The iron coordinating residue, His(45), resides on the proximal helix. The distal helix contains highly conserved glycine residues that allow the helix to flex and interact with the bound heme. Tyr(154), Lys(199), and Arg(203) orient the heme through direct interactions with the heme propionates. The rearrangements of side chains in heme-bound HO-2 compared with apoHO-2 further elucidate HO-2 heme interactions.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17965015}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17965015 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17965015}}
==About this Structure==
==About this Structure==
Line 46: Line 50:
[[Category: Structural genomics community request]]
[[Category: Structural genomics community request]]
[[Category: Structural genomics medical relevance]]
[[Category: Structural genomics medical relevance]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 16:53:48 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 10 12:38:47 2008''

Revision as of 09:38, 10 July 2008

Image:2rgz.png

Template:STRUCTURE 2rgz

Ensemble refinement of the protein crystal structure of human heme oxygenase-2 C127A (HO-2) with bound heme

Template:ABSTRACT PUBMED 17965015

About this Structure

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

Reference

Comparison of apo- and heme-bound crystal structures of a truncated human heme oxygenase-2., Bianchetti CM, Yi L, Ragsdale SW, Phillips GN Jr, J Biol Chem. 2007 Dec 28;282(52):37624-31. Epub 2007 Oct 26. PMID:17965015

Page seeded by OCA on Thu Jul 10 12:38:47 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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