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| | ==The Structure of the complex between Aha1 and HSP90== | | ==The Structure of the complex between Aha1 and HSP90== |
| - | <StructureSection load='1usv' size='340' side='right' caption='[[1usv]], [[Resolution|resolution]] 2.70Å' scene=''> | + | <StructureSection load='1usv' size='340' side='right'caption='[[1usv]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1usv]] is a 8 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=1USV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1USV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1usv]] is a 8 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=1USV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1USV FirstGlance]. <br> |
| - | </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]]</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]] 2.7Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1usv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1usv OCA], [http://pdbe.org/1usv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1usv RCSB], [http://www.ebi.ac.uk/pdbsum/1usv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1usv 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=1usv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1usv OCA], [https://pdbe.org/1usv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1usv RCSB], [https://www.ebi.ac.uk/pdbsum/1usv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1usv ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/AHA1_YEAST AHA1_YEAST] Co-chaperone that binds to the molecular chaperone HSP82 and stimulates its ATPase activity. Binding to HSP82 promotes a conformational switch in the catalytic loop of HSP82, facilitating the interaction of the catalytic 'Arg-380' with ATP in the N-terminal nucleotide-binding domain. Although not essential, it confers thermotolerance when intracellular levels of HSP82 are limiting.<ref>PMID:12504007</ref> <ref>PMID:12604615</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Heat Shock Proteins|Heat Shock Proteins]] | + | *[[Heat Shock Protein structures|Heat Shock Protein structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | + | [[Category: Large Structures]] |
| - | [[Category: Meyer, P]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Pearl, L H]] | + | [[Category: Meyer P]] |
| - | [[Category: Roe, S M]] | + | [[Category: Pearl LH]] |
| - | [[Category: Activator]] | + | [[Category: Roe SM]] |
| - | [[Category: Chaperone]]
| + | |
| - | [[Category: Chaperone-complex]]
| + | |
| - | [[Category: Hsp90]]
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| Structural highlights
Function
AHA1_YEAST Co-chaperone that binds to the molecular chaperone HSP82 and stimulates its ATPase activity. Binding to HSP82 promotes a conformational switch in the catalytic loop of HSP82, facilitating the interaction of the catalytic 'Arg-380' with ATP in the N-terminal nucleotide-binding domain. Although not essential, it confers thermotolerance when intracellular levels of HSP82 are limiting.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Hsp90 is a molecular chaperone essential for the activation and assembly of many key eukaryotic signalling and regulatory proteins. Hsp90 is assisted and regulated by co-chaperones that participate in an ordered series of dynamic multiprotein complexes, linked to Hsp90 conformationally coupled ATPase cycle. The co-chaperones Aha1 and Hch1 bind to Hsp90 and stimulate its ATPase activity. Biochemical analysis shows that this activity is dependent on the N-terminal domain of Aha1, which interacts with the central segment of Hsp90. The structural basis for this interaction is revealed by the crystal structure of the N-terminal domain (1-153) of Aha1 (equivalent to the whole of Hch1) in complex with the middle segment of Hsp90 (273-530). Structural analysis and mutagenesis show that binding of N-Aha1 promotes a conformational switch in the middle-segment catalytic loop (370-390) of Hsp90 that releases the catalytic Arg 380 and enables its interaction with ATP in the N-terminal nucleotide-binding domain of the chaperone.
Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery.,Meyer P, Prodromou C, Liao C, Hu B, Roe SM, Vaughan CK, Vlasic I, Panaretou B, Piper PW, Pearl LH EMBO J. 2004 Mar 24;23(6):1402-10. PMID:15039704[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Panaretou B, Siligardi G, Meyer P, Maloney A, Sullivan JK, Singh S, Millson SH, Clarke PA, Naaby-Hansen S, Stein R, Cramer R, Mollapour M, Workman P, Piper PW, Pearl LH, Prodromou C. Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1. Mol Cell. 2002 Dec;10(6):1307-18. PMID:12504007
- ↑ Lotz GP, Lin H, Harst A, Obermann WM. Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone. J Biol Chem. 2003 May 9;278(19):17228-35. Epub 2003 Feb 24. PMID:12604615 doi:http://dx.doi.org/10.1074/jbc.M212761200
- ↑ Meyer P, Prodromou C, Liao C, Hu B, Roe SM, Vaughan CK, Vlasic I, Panaretou B, Piper PW, Pearl LH. Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery. EMBO J. 2004 Mar 24;23(6):1402-10. PMID:15039704 doi:http://dx.doi.org/10.1038/sj.emboj.7600141
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