3qk9

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Current revision (10:48, 21 February 2024) (edit) (undo)
 
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<StructureSection load='3qk9' size='340' side='right'caption='[[3qk9]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
<StructureSection load='3qk9' size='340' side='right'caption='[[3qk9]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3qk9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QK9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QK9 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3qk9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QK9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QK9 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
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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]] 3.1&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TIM44, ISP45, MIM44, MPI1, YIL022W ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=CL:CHLORIDE+ION'>CL</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3qk9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qk9 OCA], [https://pdbe.org/3qk9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qk9 RCSB], [https://www.ebi.ac.uk/pdbsum/3qk9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qk9 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3qk9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qk9 OCA], [https://pdbe.org/3qk9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qk9 RCSB], [https://www.ebi.ac.uk/pdbsum/3qk9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qk9 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/TIM44_YEAST TIM44_YEAST]] Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. Recruits mitochondrial HSP70 and its co-chaperone (MGE1) to drive protein translocation into the matrix using ATP as an energy source.
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[https://www.uniprot.org/uniprot/TIM44_YEAST TIM44_YEAST] Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. Recruits mitochondrial HSP70 and its co-chaperone (MGE1) to drive protein translocation into the matrix using ATP as an energy source.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The protein translocations across mitochondrial membranes are carried out by specialized complexes, the Translocase of Outer Membrane (TOM) and Translocase of Inner Membrane (TIM). TIM23 translocon is responsible for translocating the mitochondrial matrix proteins across the mitochondrial inner membrane. Tim44 is an essential, peripheral membrane protein in TIM23 complex. Tim44 is tightly associated with the inner mitochondrial membrane on the matrix side. The Tim44 C-Terminal Domain (CTD) functions as an Inner Mitochondrial Membrane (IMM) anchor that recruits the Presequence protein Associated Motor (PAM) to the TIM23 channel. Using X-ray crystallographic and biochemical data, we show that the N-terminal helices A1 and A2 of Tim44 - CTD are crucial for its membrane tethering function. Based on our data, we propose a model showing how the N-terminal A1 and A2 amphipathic helices can either expose their hydrophobic face during membrane binding or conceal it in the soluble form. Therefore, the A1 and A2 helices of Tim44 may function as a membrane sensor.
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Membrane Binding Mechanism of Yeast Mitochondrial Peripheral Membrane Protein TIM44.,Cui W, Josyula R, Li J, Fu Z, Sh B Protein Pept Lett. 2011 Feb 21. PMID:21342097<ref>PMID:21342097</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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<div class="pdbe-citations 3qk9" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 18824]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Cui, W]]
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[[Category: Saccharomyces cerevisiae]]
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[[Category: Fu, Z]]
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[[Category: Cui W]]
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[[Category: Josyula, R]]
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[[Category: Fu Z]]
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[[Category: Sha, B]]
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[[Category: Josyula R]]
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[[Category: Mitochondrion]]
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[[Category: Sha B]]
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[[Category: Protein transport]]
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Current revision

Yeast Tim44 C-terminal domain complexed with Cymal-3

PDB ID 3qk9

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