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.


2v7q

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2v7q.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2v7q.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2v7q| PDB=2v7q | SCENE= }}
{{STRUCTURE_2v7q| PDB=2v7q | SCENE= }}
-
'''THE STRUCTURE OF F1-ATPASE INHIBITED BY I1-60HIS, A MONOMERIC FORM OF THE INHIBITOR PROTEIN, IF1.'''
+
===THE STRUCTURE OF F1-ATPASE INHIBITED BY I1-60HIS, A MONOMERIC FORM OF THE INHIBITOR PROTEIN, IF1.===
-
==Overview==
+
<!--
-
The structure of bovine F(1)-ATPase inhibited by a monomeric form of the inhibitor protein, IF(1), known as I1-60His, lacking most of the dimerization region, has been determined at 2.1-A resolution. The resolved region of the inhibitor from residues 8-50 consists of an extended structure from residues 8-13, followed by two alpha-helices from residues 14-18 and residues 21-50 linked by a turn. The binding site in the beta(DP)-alpha(DP) catalytic interface is complex with contributions from five different subunits of F(1)-ATPase. The longer helix extends from the external surface of F(1) via a deep groove made from helices and loops in the C-terminal domains of subunits beta(DP), alpha(DP), beta(TP), and alpha(TP) to the internal cavity surrounding the central stalk. The linker and shorter helix interact with the gamma-subunit in the central stalk, and the N-terminal region extends across the central cavity to interact with the nucleotide binding domain of the alpha(E) subunit. To form these complex interactions and penetrate into the core of the enzyme, it is likely that the initial interaction of the inhibitor with F(1) forms via the open conformation of the beta(E) subunit. Then, as two ATP molecules are hydrolyzed, the beta(E)-alpha(E) interface converts to the beta(DP)-alpha(DP) interface via the beta(TP)-alpha(TP) interface, trapping the inhibitor progressively in its binding site and a nucleotide in the catalytic site of subunit beta(DP). The inhibition probably arises by IF(1) imposing the structure and properties of the beta(TP)-alpha(TP) interface on the beta(DP)-alpha(DP) interface, thereby preventing it from hydrolyzing the bound ATP.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17895376}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17895376 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17895376}}
==About this Structure==
==About this Structure==
Line 45: Line 49:
[[Category: Transit peptide]]
[[Category: Transit peptide]]
[[Category: Transport]]
[[Category: Transport]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 18:20:17 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:21:28 2008''

Revision as of 10:21, 29 July 2008

Image:2v7q.png

Template:STRUCTURE 2v7q

THE STRUCTURE OF F1-ATPASE INHIBITED BY I1-60HIS, A MONOMERIC FORM OF THE INHIBITOR PROTEIN, IF1.

Template:ABSTRACT PUBMED 17895376

About this Structure

2V7Q is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.

Reference

How the regulatory protein, IF(1), inhibits F(1)-ATPase from bovine mitochondria., Gledhill JR, Montgomery MG, Leslie AG, Walker JE, Proc Natl Acad Sci U S A. 2007 Oct 2;104(40):15671-6. Epub 2007 Sep 25. PMID:17895376

Page seeded by OCA on Tue Jul 29 13:21:28 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2v7q"
Personal tools