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3fp2

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Current revision (06:49, 6 September 2023) (edit) (undo)
 
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<StructureSection load='3fp2' size='340' side='right'caption='[[3fp2]], [[Resolution|resolution]] 1.98&Aring;' scene=''>
<StructureSection load='3fp2' size='340' side='right'caption='[[3fp2]], [[Resolution|resolution]] 1.98&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3fp2]] 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=3FP2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FP2 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3fp2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] and [https://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=3FP2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FP2 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>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 1.98&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3fp1|3fp1]], [[3fp3|3fp3]], [[3fp4|3fp4]]</div></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>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YHR117W ([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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3fp2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fp2 OCA], [https://pdbe.org/3fp2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fp2 RCSB], [https://www.ebi.ac.uk/pdbsum/3fp2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fp2 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=3fp2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fp2 OCA], [https://pdbe.org/3fp2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fp2 RCSB], [https://www.ebi.ac.uk/pdbsum/3fp2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fp2 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/TOM71_YEAST TOM71_YEAST]] Involved in MBF1-mediated mitochondrial morphogenesis.<ref>PMID:18007655</ref> [[https://www.uniprot.org/uniprot/HSP82_YEAST HSP82_YEAST]] Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. The nucleotide-free form of the dimer is found in an open conformation in which the N-termini are not dimerized and the complex is ready for client protein binding. Binding of ATP induces large conformational changes, resulting in the formation of a ring-like closed structure in which the N-terminal domains associate intramolecularly with the middle domain and also dimerize with each other, stimulating their intrinsic ATPase activity and acting as a clamp on the substrate. Finally, ATP hydrolysis results in the release of the substrate. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Required for growth at high temperatures.<ref>PMID:17114002</ref>
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[https://www.uniprot.org/uniprot/TOM71_YEAST TOM71_YEAST] Involved in MBF1-mediated mitochondrial morphogenesis.<ref>PMID:18007655</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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: Hu, J]]
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[[Category: Saccharomyces cerevisiae]]
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[[Category: Li, J]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Qian, X]]
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[[Category: Hu J]]
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[[Category: Sha, B]]
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[[Category: Li J]]
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[[Category: Allosteric regulation]]
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[[Category: Qian X]]
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[[Category: Atp-binding]]
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[[Category: Sha B]]
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[[Category: Chaperone]]
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[[Category: Mitochondria translocation]]
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[[Category: Nucleotide-binding]]
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[[Category: Phosphoprotein]]
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[[Category: Stress response]]
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[[Category: Tom71]]
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[[Category: Tpr repeat]]
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[[Category: Transport protein]]
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Current revision

Crystal structure of Tom71 complexed with Hsp82 C-terminal fragment

PDB ID 3fp2

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