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2bsk

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2bsk]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BSK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BSK FirstGlance]. <br>
<table><tr><td colspan='2'>[[2bsk]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BSK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BSK FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bsk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bsk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bsk RCSB], [http://www.ebi.ac.uk/pdbsum/2bsk PDBsum]</span></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=2bsk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bsk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bsk RCSB], [http://www.ebi.ac.uk/pdbsum/2bsk PDBsum]</span></td></tr>
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<table>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/TIM10_HUMAN TIM10_HUMAN]] Mitochondrial intermembrane chaperone that participates in the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. May also be required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space.<ref>PMID:14726512</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Gorman, M A.]]
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[[Category: Gorman, M A]]
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[[Category: Gulbis, J M.]]
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[[Category: Gulbis, J M]]
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[[Category: Lazarus, M.]]
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[[Category: Lazarus, M]]
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[[Category: Ryan, M T.]]
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[[Category: Ryan, M T]]
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[[Category: Webb, C T.]]
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[[Category: Webb, C T]]
[[Category: Mitochondrial protein import]]
[[Category: Mitochondrial protein import]]
[[Category: Protein transport]]
[[Category: Protein transport]]

Revision as of 19:14, 25 December 2014

CRYSTAL STRUCTURE OF THE TIM9 TIM10 HEXAMERIC COMPLEX

2bsk, resolution 3.30Å

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