2iwx: Difference between revisions

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<StructureSection load='2iwx' size='340' side='right'caption='[[2iwx]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
<StructureSection load='2iwx' size='340' side='right'caption='[[2iwx]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2iwx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IWX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2IWX FirstGlance]. <br>
<table><tr><td colspan='2'>[[2iwx]] is a 1 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=2IWX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IWX FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=M1S:(5E)-14-CHLORO-15,17-DIHYDROXY-4,7,8,9,10,11-HEXAHYDRO-2-BENZOXACYCLOPENTADECINE-1,12(3H,13H)-DIONE'>M1S</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1a4h|1a4h]], [[1ah6|1ah6]], [[1ah8|1ah8]], [[1am1|1am1]], [[1amw|1amw]], [[1bgq|1bgq]], [[1hk7|1hk7]], [[1us7|1us7]], [[1usu|1usu]], [[1usv|1usv]], [[1zwh|1zwh]], [[2akp|2akp]], [[2brc|2brc]], [[2bre|2bre]], [[2cg9|2cg9]], [[2cge|2cge]], [[2cgf|2cgf]], [[2iws|2iws]], [[2iwu|2iwu]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=M1S:(5E)-14-CHLORO-15,17-DIHYDROXY-4,7,8,9,10,11-HEXAHYDRO-2-BENZOXACYCLOPENTADECINE-1,12(3H,13H)-DIONE'>M1S</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2iwx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iwx OCA], [http://pdbe.org/2iwx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2iwx RCSB], [http://www.ebi.ac.uk/pdbsum/2iwx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2iwx 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=2iwx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iwx OCA], [https://pdbe.org/2iwx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iwx RCSB], [https://www.ebi.ac.uk/pdbsum/2iwx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iwx ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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>
[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>  
== 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>
[[Category: Atcc 18824]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Pearl, L H]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Prodromou, C]]
[[Category: Pearl LH]]
[[Category: Roe, S M]]
[[Category: Prodromou C]]
[[Category: Atp-binding]]
[[Category: Roe SM]]
[[Category: Chaperone]]
[[Category: Chaperone-complex]]
[[Category: Heat shock]]
[[Category: Inhibitor]]
[[Category: Multigene family]]
[[Category: Nucleotide- binding]]

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