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.


1koi

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1koi.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1koi.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1koi| PDB=1koi | SCENE= }}
{{STRUCTURE_1koi| PDB=1koi | SCENE= }}
-
'''CRYSTAL STRUCTURE OF NITROPHORIN 4 FROM RHODNIUS PROLIXUS COMPLEXED WITH NITRIC OXIDE AT 1.08 A RESOLUTION'''
+
===CRYSTAL STRUCTURE OF NITROPHORIN 4 FROM RHODNIUS PROLIXUS COMPLEXED WITH NITRIC OXIDE AT 1.08 A RESOLUTION===
-
==Overview==
+
<!--
-
The nitrophorins are a family of proteins that use ferric heme to transport nitric oxide (NO) from the salivary glands of blood-sucking insects to their victims, resulting in vasodilation and reduced blood coagulation. We have refined atomic resolution structures of nitrophorin 4 (NP4) from Rhodnius prolixus complexed with NO (1.08 A) and NH(3) (1.15 A), yielding a highly detailed picture of the iron coordination sphere. In NP4-NO, the NO nitrogen is coordinated to iron (Fe-N distance = 1.66 A) and is somewhat bent (Fe-N-O angle = 156 degrees ), with bending occurring in the same plane as the proximal histidine ring. The Fe(NO)(heme)(His) coordination geometry is unusual but consistent with an Fe(III) oxidation state that is stabilized by a highly ruffled heme. Heme ruffling occurs in both structures, apparently due to close contacts between the heme and leucines 123 and 133, but increases on binding NO even though the steric contacts have not changed. We also report the structure of NP4 in complexes with histamine (1.50 A) and imidazole (1.27 A). Unexpectedly, two mobile loops that rearrange to pack against the bound NO in NP4-NO, also rearrange in the NP4-imidazole complex. This conformational change is apparently driven by the nonpolar nature of the NO and imidazole (as bound) ligands. Taken together, the desolvation of the NO binding pocket through a change in protein conformation, and the bending of the NO moiety, possibly through protein-assisted heme ruffling, may lead to a nitrosyl-heme complex that is unusually resistant to autoreduction.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11560480}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11560480 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11560480}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Lipocalin]]
[[Category: Lipocalin]]
[[Category: Nitric oxide transport]]
[[Category: Nitric oxide transport]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:59:06 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:39:18 2008''

Revision as of 07:39, 2 July 2008

Image:1koi.png

Template:STRUCTURE 1koi

CRYSTAL STRUCTURE OF NITROPHORIN 4 FROM RHODNIUS PROLIXUS COMPLEXED WITH NITRIC OXIDE AT 1.08 A RESOLUTION

Template:ABSTRACT PUBMED 11560480

About this Structure

1KOI is a Single protein structure of sequence from Rhodnius prolixus. This structure supersedes the now removed PDB entry 1ikh. Full crystallographic information is available from OCA.

Reference

Ligand-induced heme ruffling and bent no geometry in ultra-high-resolution structures of nitrophorin 4., Roberts SA, Weichsel A, Qiu Y, Shelnutt JA, Walker FA, Montfort WR, Biochemistry. 2001 Sep 25;40(38):11327-37. PMID:11560480

Page seeded by OCA on Wed Jul 2 10:39:18 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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