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.


1p3u

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1p3u.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1p3u.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1p3u| PDB=1p3u | SCENE= }}
{{STRUCTURE_1p3u| PDB=1p3u | SCENE= }}
-
'''Crystal Structures of the NO-and CO-Bound Heme Oxygenase From Neisseria Meningitidis: Implications for Oxygen Activation'''
+
===Crystal Structures of the NO-and CO-Bound Heme Oxygenase From Neisseria Meningitidis: Implications for Oxygen Activation===
-
==Overview==
+
<!--
-
Heme oxygenases catalyze the oxidation of heme to biliverdin, carbon monoxide, and free iron while playing a critical role in mammalian heme homeostasis. Pathogenic bacteria such as Neisseriae meningitidis also produce heme oxygenase as part of a mechanism to mine host iron. The key step in heme oxidation is the regioselective oxidation of the heme alpha-meso-carbon by an activated Fe(III)-OOH complex. The structures of various diatomic ligands bound to the heme iron can mimic the dioxygen complex and provide important insights on the mechanism of O2 activation. Here we report the crystal structures of N. meningitidis heme oxygenase (nm-HO) in the Fe(II), Fe(II)-CO, and Fe(II)-NO states and compare these to the NO complex of human heme oxygenase-1 (Lad, L., Wang, J., Li, H., Friedman, J., Bhaskar, B., Ortiz de Montellano, P. R., and Poulos, T. L. (2003) J. Mol. Biol. 330, 527-538). Coordination of NO or CO results in a reorientation of Arg-77 that enables Arg-77 to participate in an active site H-bonded network involving a series of water molecules. One of these water molecules directly H-bonds to the Fe(II)-linked ligand and very likely serves as the proton source required for oxygen activation. Although the active site residues differ between nm-HO and human HO-1, the close similarity in the H-bonded water network suggests a common mechanism shared by all heme oxygenases.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12819228}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12819228 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12819228}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Heme degradation]]
[[Category: Heme degradation]]
[[Category: Heme oxygenase]]
[[Category: Heme oxygenase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:39:05 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:38:33 2008''

Revision as of 04:38, 29 July 2008

Image:1p3u.png

Template:STRUCTURE 1p3u

Crystal Structures of the NO-and CO-Bound Heme Oxygenase From Neisseria Meningitidis: Implications for Oxygen Activation

Template:ABSTRACT PUBMED 12819228

About this Structure

1P3U is a Single protein structure of sequence from Neisseria meningitidis. Full crystallographic information is available from OCA.

Reference

Crystal structures of the NO- and CO-bound heme oxygenase from Neisseriae meningitidis. Implications for O2 activation., Friedman J, Lad L, Deshmukh R, Li H, Wilks A, Poulos TL, J Biol Chem. 2003 Sep 5;278(36):34654-9. Epub 2003 Jun 22. PMID:12819228

Page seeded by OCA on Tue Jul 29 07:38:33 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1p3u"
Personal tools