1zht: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
No edit summary
Line 1: Line 1:
[[Image:1zht.gif|left|200px]]
{{Seed}}
[[Image:1zht.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1zht|  PDB=1zht  |  SCENE=  }}  
{{STRUCTURE_1zht|  PDB=1zht  |  SCENE=  }}  


'''Structure of yeast oxysterol binding protein Osh4 in complex with 7-hydroxycholesterol'''
===Structure of yeast oxysterol binding protein Osh4 in complex with 7-hydroxycholesterol===




==Overview==
<!--
The oxysterol-binding-protein (OSBP)-related proteins (ORPs) are conserved from yeast to humans, and are implicated in the regulation of sterol homeostasis and in signal transduction pathways. Here we report the structure of the full-length yeast ORP Osh4 (also known as Kes1) at 1.5-1.9 A resolution in complexes with ergosterol, cholesterol, and 7-, 20- and 25-hydroxycholesterol. We find that a single sterol molecule binds within a hydrophobic tunnel in a manner consistent with a transport function for ORPs. The entrance is blocked by a flexible amino-terminal lid and surrounded by basic residues that are critical for Osh4 function. The structure of the open state of a lid-truncated form of Osh4 was determined at 2.5 A resolution. Structural analysis and limited proteolysis show that sterol binding closes the lid and stabilizes a conformation favouring transport across aqueous barriers and signal transmission. The structure of Osh4 in the absence of ligand exposes potential phospholipid-binding sites that are positioned for membrane docking and sterol exchange. On the basis of these observations, we propose a model in which sterol and membrane binding promote reciprocal conformational changes that facilitate a sterol transfer and signalling cycle.
The line below this paragraph, {{ABSTRACT_PUBMED_16136145}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 16136145 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_16136145}}


==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Raychaudhuri, S.]]
[[Category: Raychaudhuri, S.]]
[[Category: Oxysterol sterol binding protein cholesterol]]
[[Category: Oxysterol sterol binding protein cholesterol]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 17:38:36 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 17:11:58 2008''

Revision as of 14:11, 28 July 2008

File:1zht.png

Template:STRUCTURE 1zht

Structure of yeast oxysterol binding protein Osh4 in complex with 7-hydroxycholesterol

Template:ABSTRACT PUBMED 16136145

About this Structure

1ZHT is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Structural mechanism for sterol sensing and transport by OSBP-related proteins., Im YJ, Raychaudhuri S, Prinz WA, Hurley JH, Nature. 2005 Sep 1;437(7055):154-8. PMID:16136145

Page seeded by OCA on Mon Jul 28 17:11:58 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1zht&oldid=708617"