1am1

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[[Image:1am1.jpg|left|200px]]
 
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{{Structure
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==ATP BINDING SITE IN THE HSP90 MOLECULAR CHAPERONE==
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|PDB= 1am1 |SIZE=350|CAPTION= <scene name='initialview01'>1am1</scene>, resolution 2.00&Aring;
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<StructureSection load='1am1' size='340' side='right'caption='[[1am1]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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|SITE= <scene name='pdbsite=S1:Atp+Binding+Site'>S1</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5&#39;-DIPHOSPHATE'>ADP</scene>
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<table><tr><td colspan='2'>[[1am1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. The December 2008 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Hsp90'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2008_12 10.2210/rcsb_pdb/mom_2008_12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AM1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AM1 FirstGlance]. <br>
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|ACTIVITY=
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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]] 2&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr>
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|DOMAIN=
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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=1am1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1am1 OCA], [https://pdbe.org/1am1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1am1 RCSB], [https://www.ebi.ac.uk/pdbsum/1am1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1am1 ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1am1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1am1 OCA], [http://www.ebi.ac.uk/pdbsum/1am1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1am1 RCSB]</span>
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== Function ==
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}}
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[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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== 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/am/1am1_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=1am1 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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Hsp90 molecular chaperones in eukaryotic cells play essential roles in the folding and activation of a range of client proteins involved in cell cycle regulation, steroid hormone responsiveness, and signal transduction. The biochemical mechanism of Hsp90 is poorly understood, and the involvement of ATP in particular is controversial. Crystal structures of complexes between the N-terminal domain of the yeast Hsp90 chaperone and ADP/ATP unambiguously identify a specific adenine nucleotide binding site homologous to the ATP-binding site of DNA gyrase B. This site is the same as that identified for the antitumor agent geldanamycin, suggesting that geldanamycin acts by blocking the binding of nucleotides to Hsp90 and not the binding of incompletely folded client polypeptides as previously suggested. These results finally resolve the question of the direct involvement of ATP in Hsp90 function.
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'''ATP BINDING SITE IN THE HSP90 MOLECULAR CHAPERONE'''
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Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone.,Prodromou C, Roe SM, O'Brien R, Ladbury JE, Piper PW, Pearl LH Cell. 1997 Jul 11;90(1):65-75. PMID:9230303<ref>PMID:9230303</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 1am1" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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Hsp90 molecular chaperones in eukaryotic cells play essential roles in the folding and activation of a range of client proteins involved in cell cycle regulation, steroid hormone responsiveness, and signal transduction. The biochemical mechanism of Hsp90 is poorly understood, and the involvement of ATP in particular is controversial. Crystal structures of complexes between the N-terminal domain of the yeast Hsp90 chaperone and ADP/ATP unambiguously identify a specific adenine nucleotide binding site homologous to the ATP-binding site of DNA gyrase B. This site is the same as that identified for the antitumor agent geldanamycin, suggesting that geldanamycin acts by blocking the binding of nucleotides to Hsp90 and not the binding of incompletely folded client polypeptides as previously suggested. These results finally resolve the question of the direct involvement of ATP in Hsp90 function.
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*[[Heat Shock Protein structures|Heat Shock Protein structures]]
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== References ==
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==About this Structure==
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<references/>
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1AM1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AM1 OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Hsp90]]
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Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone., Prodromou C, Roe SM, O'Brien R, Ladbury JE, Piper PW, Pearl LH, Cell. 1997 Jul 11;90(1):65-75. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9230303 9230303]
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[[Category: Large Structures]]
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[[Category: RCSB PDB Molecule of the Month]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Pearl LH]]
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[[Category: Pearl, L H.]]
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[[Category: Prodromou C]]
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[[Category: Prodromou, C.]]
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[[Category: Roe SM]]
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[[Category: Roe, S M.]]
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[[Category: chaperone]]
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[[Category: nucleotide binding site]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:43:02 2008''
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Current revision

ATP BINDING SITE IN THE HSP90 MOLECULAR CHAPERONE

PDB ID 1am1

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