4hse: Difference between revisions

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==Crystal structure of ClpB NBD1 in complex with guanidinium chloride and ADP==
==Crystal structure of ClpB NBD1 in complex with guanidinium chloride and ADP==
<StructureSection load='4hse' size='340' side='right' caption='[[4hse]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='4hse' size='340' side='right'caption='[[4hse]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4hse]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thet8 Thet8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HSE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HSE FirstGlance]. <br>
<table><tr><td colspan='2'>[[4hse]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HSE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HSE 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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GAI:GUANIDINE'>GAI</scene></td></tr>
</td></tr><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>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GAI:GUANIDINE'>GAI</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1qvr|1qvr]], [[1jbk|1jbk]]</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=4hse FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hse OCA], [https://pdbe.org/4hse PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hse RCSB], [https://www.ebi.ac.uk/pdbsum/4hse PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hse ProSAT]</span></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">clpB, TTHA1487 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=300852 THET8])</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=4hse FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hse OCA], [http://pdbe.org/4hse PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4hse RCSB], [http://www.ebi.ac.uk/pdbsum/4hse PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4hse ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/CLPB_THET8 CLPB_THET8]] Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK.<ref>PMID:10377389</ref>
[https://www.uniprot.org/uniprot/CLPB_THET8 CLPB_THET8] Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK.<ref>PMID:10377389</ref>  
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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==See Also==
==See Also==
*[[Heat Shock Proteins|Heat Shock Proteins]]
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
*[[3D structures of ClpB|3D structures of ClpB]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Thet8]]
[[Category: Large Structures]]
[[Category: Reinstein, J]]
[[Category: Thermus thermophilus HB8]]
[[Category: Schlichting, I]]
[[Category: Reinstein J]]
[[Category: Werbeck, N D]]
[[Category: Schlichting I]]
[[Category: Zeymer, C]]
[[Category: Werbeck ND]]
[[Category: Aaa+ protein]]
[[Category: Zeymer C]]
[[Category: Chaperone]]
[[Category: Molecular chaperone]]
[[Category: Nucleotide binding domain]]