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2bsk

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{{Seed}}
 
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[[Image:2bsk.png|left|200px]]
 
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==Crystal structure of the TIM9 Tim10 hexameric complex==
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The line below this paragraph, containing "STRUCTURE_2bsk", creates the "Structure Box" on the page.
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<StructureSection load='2bsk' size='340' side='right'caption='[[2bsk]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2bsk]] is a 6 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=2BSK FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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{{STRUCTURE_2bsk| PDB=2bsk | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2bsk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bsk OCA], [https://pdbe.org/2bsk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bsk RCSB], [https://www.ebi.ac.uk/pdbsum/2bsk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bsk ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TIM9_HUMAN TIM9_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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bs/2bsk_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2bsk ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Import of proteins into mitochondria occurs by coordinated actions of preprotein translocases in the outer and inner membranes. Tim9 and Tim10 are translocase components of the intermembrane space, related to deafness-dystonia peptide 1 (DDP1). They coassemble into a hexamer, TIM9.10, which captures and chaperones precursors of inner membrane metabolite carriers as they exit the TOM channel in the outer membrane. The crystal structure of TIM9.10 reveals a previously undescribed alpha-propeller topology in which helical "blades" radiate from a narrow central pore lined with polar residues. The propeller blades are reminiscent of "tentacles" in chaperones Skp and prefoldin. In each TIM9.10 subunit, a signature "twin CX3C" motif forms two intramolecular disulfides. There is no obvious binding pocket for precursors, which we suggest employ the chaperone-like tentacles of TIM9.10 as surrogate lipid contacts. The first reported crystal structure of a mitochondrial translocase assembly provides insights into selectivity and regulation of precursor import.
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===CRYSTAL STRUCTURE OF THE TIM9 TIM10 HEXAMERIC COMPLEX===
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Crystal structure of the mitochondrial chaperone TIM9.10 reveals a six-bladed alpha-propeller.,Webb CT, Gorman MA, Lazarou M, Ryan MT, Gulbis JM Mol Cell. 2006 Jan 6;21(1):123-33. PMID:16387659<ref>PMID:16387659</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_16387659}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2bsk" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 16387659 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_16387659}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2BSK is a [[Protein complex]] structure of sequences 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].
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==Reference==
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Crystal structure of the mitochondrial chaperone TIM9.10 reveals a six-bladed alpha-propeller., Webb CT, Gorman MA, Lazarou M, Ryan MT, Gulbis JM, Mol Cell. 2006 Jan 6;21(1):123-33. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16387659 16387659]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Gorman, M A.]]
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[[Category: Gorman MA]]
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[[Category: Gulbis, J M.]]
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[[Category: Gulbis JM]]
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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 MT]]
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[[Category: Webb, C T.]]
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[[Category: Webb CT]]
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[[Category: Protein transport]]
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[[Category: Tim9,tim10,mitochondrial protein import,tim complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 10:36:10 2008''
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Current revision

Crystal structure of the TIM9 Tim10 hexameric complex

PDB ID 2bsk

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