2v7z: Difference between revisions
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==CRYSTAL STRUCTURE OF THE 70-KDA HEAT SHOCK COGNATE PROTEIN FROM RATTUS NORVEGICUS IN POST-ATP HYDROLYSIS STATE== | ==CRYSTAL STRUCTURE OF THE 70-KDA HEAT SHOCK COGNATE PROTEIN FROM RATTUS NORVEGICUS IN POST-ATP HYDROLYSIS STATE== | ||
<StructureSection load='2v7z' size='340' side='right' caption='[[2v7z]], [[Resolution|resolution]] 3.50Å' scene=''> | <StructureSection load='2v7z' size='340' side='right' caption='[[2v7z]], [[Resolution|resolution]] 3.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2v7z]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2v7z]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V7Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2V7Z FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=2v7z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v7z OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2v7z RCSB], [http://www.ebi.ac.uk/pdbsum/2v7z PDBsum]</span></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=2v7z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v7z OCA], [http://pdbe.org/2v7z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2v7z RCSB], [http://www.ebi.ac.uk/pdbsum/2v7z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2v7z ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</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/ | </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=2v7z ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 2v7z" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Buffalo rat]] | ||
[[Category: Chang, Y W]] | [[Category: Chang, Y W]] | ||
[[Category: Hsiao, C D]] | [[Category: Hsiao, C D]] | ||
Revision as of 17:11, 5 August 2016
CRYSTAL STRUCTURE OF THE 70-KDA HEAT SHOCK COGNATE PROTEIN FROM RATTUS NORVEGICUS IN POST-ATP HYDROLYSIS STATECRYSTAL STRUCTURE OF THE 70-KDA HEAT SHOCK COGNATE PROTEIN FROM RATTUS NORVEGICUS IN POST-ATP HYDROLYSIS STATE
Structural highlights
Function[HSP7C_RAT] Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Chaperone. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex (By similarity). 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 PubMedThe 70-kDa heat shock proteins (Hsp70s) are highly conserved ATP-dependent molecular chaperones composed of an N-terminal nucleotide binding domain (NBD) and a C-terminal protein substrate binding domain (SBD) in a bilobate structure. Interdomain communication and nucleotide-dependent structural motions are critical for Hsp70 chaperone functions. Our understanding of these functions remains elusive due to insufficient structural information on intact Hsp70s that represent the different states of the chaperone cycle. We report here the crystal structures of DnaK from Geobacillus kaustophilus HTA426 bound with ADP-Mg(2+)-P(i) at 2.37A and the 70-kDa heat shock cognate protein from Rattus norvegicus bound with ADP-P(i) at 3.5A(.) The NBD and SBD in these structures are significantly separated from each other, and they might depict the ADP-bound conformation. Moreover, a Trp reporter was introduced at the potential interface region between NBD and the interdomain linker of GkDnaK to probe environmental changes. Results from fluorescence measurements support the notion that substrate binding enhances the domain-disjoining behavior of Hsp70 chaperones. Crystal structures of the 70-kDa heat shock proteins in domain disjoining conformation.,Chang YW, Sun YJ, Wang C, Hsiao CD J Biol Chem. 2008 May 30;283(22):15502-11. Epub 2008 Apr 8. PMID:18400763[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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