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3ulc

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{{STRUCTURE_3ulc| PDB=3ulc | SCENE= }}
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==Crystal structure of the pleckstrin homology domain of Saccharomyces cerevisiae Avo1, a TORC2 subunit, in the P3121 crystal form==
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===Crystal structure of the pleckstrin homology domain of Saccharomyces cerevisiae Avo1, a TORC2 subunit, in the P3121 crystal form===
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<StructureSection load='3ulc' size='340' side='right' caption='[[3ulc]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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{{ABSTRACT_PUBMED_22505404}}
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3ulc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ULC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ULC FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ulb|3ulb]]</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AVO1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Saccharomyces cerevisiae S288c])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ulc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ulc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ulc RCSB], [http://www.ebi.ac.uk/pdbsum/3ulc PDBsum]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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In eukaryotes, multiprotein complexes termed TOR complex 1 (TORC1) and TOR complex 2 (TORC2) function as major regulators of cell growth, metabolism and ageing. The C-terminal domain of the Saccharomyces cerevisiae TORC2 component Avo1 is required for plasma-membrane localization of TORC2 and is essential for yeast viability. X-ray crystal structures of the C-terminal domain of Avo1 and of its human orthologue Sin1 have been determined. The structures show that the C-termini of Avo1 and Sin1 both have the pleckstrin homology (PH) domain fold. Comparison with known PH-domain structures suggests a putative binding site for phosphoinositides.
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==Function==
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Structures of the pleckstrin homology domain of Saccharomyces cerevisiae Avo1 and its human orthologue Sin1, an essential subunit of TOR complex 2.,Pan D, Matsuura Y Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Apr 1;68(Pt 4):386-92., Epub 2012 Mar 27. PMID:22505404<ref>PMID:22505404</ref>
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[[http://www.uniprot.org/uniprot/AVO1_YEAST AVO1_YEAST]] Component of TORC2, which regulates cell cycle-dependent polarization of the actin-cytoskeleton and cell wall integrity. TORC2 controls polarity of the actin cytoskeleton, which is required for orienting the secretory pathway toward discrete growth sites, via the RHO1/PKC1/MAPK cell integrity pathway.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[3ulc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ULC OCA].
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</div>
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:022505404</ref><references group="xtra"/><references/>
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__TOC__
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</StructureSection>
[[Category: Saccharomyces cerevisiae s288c]]
[[Category: Saccharomyces cerevisiae s288c]]
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[[Category: Matsuura, Y.]]
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[[Category: Matsuura, Y]]
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[[Category: Pan, D.]]
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[[Category: Pan, D]]
[[Category: Membrane localization]]
[[Category: Membrane localization]]
[[Category: Membrane protein]]
[[Category: Membrane protein]]
[[Category: Ph domain]]
[[Category: Ph domain]]

Revision as of 06:28, 21 December 2014

Crystal structure of the pleckstrin homology domain of Saccharomyces cerevisiae Avo1, a TORC2 subunit, in the P3121 crystal form

3ulc, resolution 2.80Å

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