1aua: Difference between revisions
New page: left|200px<br /><applet load="1aua" size="450" color="white" frame="true" align="right" spinBox="true" caption="1aua, resolution 2.5Å" /> '''PHOSPHATIDYLINOSITOL ... |
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[[Image:1aua.gif|left|200px]]<br /><applet load="1aua" size=" | [[Image:1aua.gif|left|200px]]<br /><applet load="1aua" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1aua, resolution 2.5Å" /> | caption="1aua, resolution 2.5Å" /> | ||
'''PHOSPHATIDYLINOSITOL TRANSFER PROTEIN SEC14P FROM SACCHAROMYCES CEREVISIAE'''<br /> | '''PHOSPHATIDYLINOSITOL TRANSFER PROTEIN SEC14P FROM SACCHAROMYCES CEREVISIAE'''<br /> | ||
==Overview== | ==Overview== | ||
The yeast phosphatidylinositol-transfer protein (Sec14) catalyses exchange | 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== | ==About this Structure== | ||
1AUA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with BOG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1AUA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=BOG:'>BOG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AUA OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bankaitis, V | [[Category: Bankaitis, V A.]] | ||
[[Category: Luo, M.]] | [[Category: Luo, M.]] | ||
[[Category: Phillips, S | [[Category: Phillips, S E.]] | ||
[[Category: Sha, B.]] | [[Category: Sha, B.]] | ||
[[Category: BOG]] | [[Category: BOG]] | ||
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[[Category: phospholipid-binding protein]] | [[Category: phospholipid-binding protein]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:48:21 2008'' | ||
Revision as of 09:48, 21 February 2008
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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 with BOG as ligand. 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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