2e2z

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{{Seed}}
 
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[[Image:2e2z.png|left|200px]]
 
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==Solution NMR structure of yeast Tim15, co-chaperone of mitochondrial Hsp70==
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The line below this paragraph, containing "STRUCTURE_2e2z", creates the "Structure Box" on the page.
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<StructureSection load='2e2z' size='340' side='right'caption='[[2e2z]]' 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'>[[2e2z]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E2Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E2Z 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">Solution NMR</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=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_2e2z| PDB=2e2z | 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=2e2z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e2z OCA], [https://pdbe.org/2e2z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e2z RCSB], [https://www.ebi.ac.uk/pdbsum/2e2z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e2z ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ZIM17_YEAST ZIM17_YEAST] Involved in protein import into mitochondria. Acts as a Hsp70-specific chaperone that prevents self-aggregation of the matrix Hsp70 chaperones SSC1 (mtHSP70) and SSQ1, thereby maintaining their function in mitochondrial protein import and Fe/S protein biosynthesis. May act together with PAM18 as co-chaperone to facilitate recognition and folding of imported proteins by SSC1 in the mitochondrial matrix.<ref>PMID:15383543</ref> <ref>PMID:15642367</ref> <ref>PMID:15719019</ref> <ref>PMID:15992824</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/e2/2e2z_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2e2z 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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Mitochondrial heat-shock protein 70 (mtHsp70) and its partner proteins drive protein import into the matrix. Tim15/Zim17/Hep1 is a mtHsp70 partner protein on the matrix side of the inner mitochondrial membrane. We determined the nuclear magnetic resonance (NMR) structure of the core domain of Tim15. On the basis of the NMR structure, we created Tim15 mutants and tested their ability to complement the functional defects of Tim15 depletion and to suppress self-aggregation of mtHsp70 in vivo. A pair of basic residues, Arg 106 and His 107, conserved Asp 111 and flexible loop 133-137, and were important (Arg 106-His 107 pair and Asp 111) or partly important (the loop 133-137) for yeast cell growth, mitochondrial protein import and the suppression of mtHsp70 aggregation. Therefore, the function of Tim15 in yeast cell growth is well correlated with its ability to suppress mtHsp70 aggregation, although it is still unknown whether inhibition of mtHsp70 aggregation is the primary function of Tim15.
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===Solution NMR structure of yeast Tim15, co-chaperone of mitochondrial Hsp70===
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Structural basis of functional cooperation of Tim15/Zim17 with yeast mitochondrial Hsp70.,Momose T, Ohshima C, Maeda M, Endo T EMBO Rep. 2007 Jul;8(7):664-70. Epub 2007 Jun 15. PMID:17571076<ref>PMID:17571076</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_17571076}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2e2z" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 17571076 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17571076}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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2E2Z is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E2Z OCA].
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==Reference==
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Structural basis of functional cooperation of Tim15/Zim17 with yeast mitochondrial Hsp70., Momose T, Ohshima C, Maeda M, Endo T, EMBO Rep. 2007 Jul;8(7):664-70. Epub 2007 Jun 15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17571076 17571076]
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Endo T]]
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[[Category: Endo, T.]]
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[[Category: Maeda M]]
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[[Category: Maeda, M.]]
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[[Category: Momose T]]
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[[Category: Momose, T.]]
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[[Category: Ohshima C]]
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[[Category: Ohshima, C.]]
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[[Category: Chaperone regulator]]
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[[Category: Protein import]]
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[[Category: Protein transport]]
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[[Category: Zinc finger]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:27:13 2008''
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Current revision

Solution NMR structure of yeast Tim15, co-chaperone of mitochondrial Hsp70

PDB ID 2e2z

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