1aua
From Proteopedia
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- | [[Image:1aua.gif|left|200px]] | + | [[Image:1aua.gif|left|200px]] |
- | + | ||
- | '''PHOSPHATIDYLINOSITOL TRANSFER PROTEIN SEC14P FROM SACCHAROMYCES CEREVISIAE''' | + | {{Structure |
+ | |PDB= 1aua |SIZE=350|CAPTION= <scene name='initialview01'>1aua</scene>, resolution 2.5Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= SEC14 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | ||
+ | }} | ||
+ | |||
+ | '''PHOSPHATIDYLINOSITOL TRANSFER PROTEIN SEC14P FROM SACCHAROMYCES CEREVISIAE''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1AUA is a [ | + | 1AUA 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=1AUA OCA]. |
==Reference== | ==Reference== | ||
- | Crystal structure of the Saccharomyces cerevisiae phosphatidylinositol-transfer protein., Sha B, Phillips SE, Bankaitis VA, Luo M, Nature. 1998 Jan 29;391(6666):506-10. PMID:[http:// | + | Crystal structure of the Saccharomyces cerevisiae phosphatidylinositol-transfer protein., Sha B, Phillips SE, Bankaitis VA, Luo M, Nature. 1998 Jan 29;391(6666):506-10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9461221 9461221] |
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: phospholipid-binding protein]] | [[Category: phospholipid-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 10:02:20 2008'' |
Revision as of 08:02, 20 March 2008
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, resolution 2.5Å | |||||||
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Ligands: | |||||||
Gene: | SEC14 (Saccharomyces cerevisiae) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
PHOSPHATIDYLINOSITOL TRANSFER PROTEIN SEC14P FROM SACCHAROMYCES CEREVISIAE
Overview
The yeast phosphatidylinositol-transfer protein (Sec14) catalyses exchange of phosphatidylinositol and phosphatidylcholine between membrane bilayers in vitro. In vivo, Sec14 activity is essential for vesicle budding from the Golgi complex. Here we report a three-dimensional structure for Sec14 at 2.5 A resolution. Sec14 consists of twelve alpha-helices, six beta-strands, eight 3(10)-helices and has two distinct domains. The carboxy-terminal domain forms a hydrophobic pocket which, in the crystal structure, is occupied by two molecules of n-octyl-beta-D-glucopyranoside and represents the phospholipid-binding domain. This pocket is reinforced by a string motif whose disruption in a sec14 temperature-sensitive mutant results in destabilization of the phospholipid-binding domain. Finally, we have identified an unusual surface helix that may play a critical role in driving Sec14-mediated phospholipid exchange. From this structure, we derive the first molecular clues into how a phosphatidylinositol-transfer protein functions.
About this Structure
1AUA is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Crystal structure of the Saccharomyces cerevisiae phosphatidylinositol-transfer protein., Sha B, Phillips SE, Bankaitis VA, Luo M, Nature. 1998 Jan 29;391(6666):506-10. PMID:9461221
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