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.


2o5m

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2o5m.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2o5m.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2o5m| PDB=2o5m | SCENE= }}
{{STRUCTURE_2o5m| PDB=2o5m | SCENE= }}
-
'''Manganese horse heart myoglobin, azide modified'''
+
===Manganese horse heart myoglobin, azide modified===
-
==Overview==
+
<!--
-
Nitrite is now recognized as a storage pool of bioactive nitric oxide (NO). Hemoglobin (Hb) and myoglobin (Mb) convert, under certain conditions, nitrite to NO. This newly discovered nitrite reductase activity of Hb and Mb provides an attractive alternative to mammalian NO synthesis from the NO synthase pathway that requires dioxygen. We recently reported the X-ray crystal structure of the nitrite adduct of ferric horse heart Mb, and showed that the nitrite ligand binds in an unprecedented O-binding (nitrito) mode to the d(5) ferric center in Mb(III)(ONO) [D.M. Copeland, A. Soares, A.H. West, G.B. Richter-Addo, J. Inorg. Biochem. 100 (2006) 1413-1425]. We also showed that the distal pocket in Mb allows for different conformations of the NO ligand (120 degrees and 144 degrees ) in Mb(II)NO depending on the mode of preparation of the compound. In this article, we report the crystal structures of the nitrite and NO adducts of manganese-substituted hh Mb (a d(4) system) and of the nitrite adduct of cobalt-substituted hh Mb (a d(6) system). We show that the distal His64 residue directs the nitrite ligand towards the rare nitrito O-binding mode in Mn(III)Mb and Co(III)Mb. We also report that the distal pocket residues allow a stabilization of an unprecendented bent MnNO moiety in Mn(II)MbNO. These crystal structural data, when combined with the data for the aquo, methanol, and azide MnMb derivatives, provide information on the role of distal pocket residues in the observed binding modes of nitrite and NO ligands to wild-type and metal-substituted Mb.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17905436}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17905436 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17905436}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Manganese protoporphyrin ix]]
[[Category: Manganese protoporphyrin ix]]
[[Category: Oxygen storage/transport complex]]
[[Category: Oxygen storage/transport complex]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 10:21:26 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:49:53 2008''

Revision as of 05:49, 29 July 2008

Image:2o5m.png

Template:STRUCTURE 2o5m

Manganese horse heart myoglobin, azide modified

Template:ABSTRACT PUBMED 17905436

About this Structure

2O5M is a Single protein structure of sequence from Equus caballus. Full crystallographic information is available from OCA.

Reference

Crystal structures of manganese- and cobalt-substituted myoglobin in complex with NO and nitrite reveal unusual ligand conformations., Zahran ZN, Chooback L, Copeland DM, West AH, Richter-Addo GB, J Inorg Biochem. 2008 Feb;102(2):216-33. Epub 2007 Aug 25. PMID:17905436

Page seeded by OCA on Tue Jul 29 08:49:53 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2o5m"
Personal tools