1zhy
From Proteopedia
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| - | [[Image:1zhy.gif|left|200px]] | + | [[Image:1zhy.gif|left|200px]] |
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| - | '''Structure of yeast oxysterol binding protein Osh4 in complex with cholesterol''' | + | {{Structure |
| + | |PDB= 1zhy |SIZE=350|CAPTION= <scene name='initialview01'>1zhy</scene>, resolution 1.60Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=PB:LEAD+(II)+ION'>PB</scene> and <scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= OSH4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | ||
| + | }} | ||
| + | |||
| + | '''Structure of yeast oxysterol binding protein Osh4 in complex with cholesterol''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1ZHY is a [ | + | 1ZHY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZHY OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16136145 16136145] |
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: sterol binding protein]] | [[Category: sterol binding protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:35:40 2008'' |
Revision as of 13:35, 20 March 2008
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| , resolution 1.60Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | OSH4 (Saccharomyces cerevisiae) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of yeast oxysterol binding protein Osh4 in complex with cholesterol
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.
About this Structure
1ZHY 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
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