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| | ==Crystal Structure of the N-terminal Domain of HtpG, the Escherichia coli Hsp90, Bound to ADP== | | ==Crystal Structure of the N-terminal Domain of HtpG, the Escherichia coli Hsp90, Bound to ADP== |
| - | <StructureSection load='2ior' size='340' side='right' caption='[[2ior]], [[Resolution|resolution]] 1.65Å' scene=''> | + | <StructureSection load='2ior' size='340' side='right'caption='[[2ior]], [[Resolution|resolution]] 1.65Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2ior]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IOR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2IOR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2ior]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IOR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IOR 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=HEZ:HEXANE-1,6-DIOL'>HEZ</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 1.65Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1y4u|1y4u]], [[1y4s|1y4s]], [[2iop|2iop]], [[2ioq|2ioq]]</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=HEZ:HEXANE-1,6-DIOL'>HEZ</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">htpG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=2ior FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ior OCA], [https://pdbe.org/2ior PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ior RCSB], [https://www.ebi.ac.uk/pdbsum/2ior PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ior ProSAT]</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=2ior FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ior OCA], [http://pdbe.org/2ior PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ior RCSB], [http://www.ebi.ac.uk/pdbsum/2ior PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ior ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/HTPG_ECOLI HTPG_ECOLI]] Molecular chaperone. Has ATPase activity.[HAMAP-Rule:MF_00505] | + | [https://www.uniprot.org/uniprot/HTPG_ECOLI HTPG_ECOLI] Molecular chaperone. Has ATPase activity.[HAMAP-Rule:MF_00505] |
| | == 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: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| - | [[Category: Agard, D A]] | + | [[Category: Large Structures]] |
| - | [[Category: Harris, S F]] | + | [[Category: Agard DA]] |
| - | [[Category: Shiau, A K]] | + | [[Category: Harris SF]] |
| - | [[Category: Chaperone]] | + | [[Category: Shiau AK]] |
| - | [[Category: Heat shock protein]]
| + | |
| - | [[Category: Hsp90]]
| + | |
| Structural highlights
Function
HTPG_ECOLI Molecular chaperone. Has ATPase activity.[HAMAP-Rule:MF_00505]
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
In eukaryotes, the ubiquitous and abundant members of the 90 kilodalton heat-shock protein (hsp90) chaperone family facilitate the folding and conformational changes of a broad array of proteins important in cell signaling, proliferation, and survival. Here we describe the effects of nucleotides on the structure of full-length HtpG, the Escherichia coli hsp90 ortholog. By electron microscopy, the nucleotide-free, AMPPNP bound, and ADP bound states of HtpG adopt completely distinct conformations. Structural characterization of nucleotide-free and ADP bound HtpG was extended to higher resolution by X-ray crystallography. In the absence of nucleotide, HtpG exhibits an "open" conformation in which the three domains of each monomer present hydrophobic elements into the large cleft formed by the dimer. By contrast, ADP binding drives dramatic conformational changes that allow these hydrophobic elements to converge and shield each other from solvent, suggesting a mechanism by which nucleotides could control client protein binding and release.
Structural Analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements.,Shiau AK, Harris SF, Southworth DR, Agard DA Cell. 2006 Oct 20;127(2):329-40. PMID:17055434[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Shiau AK, Harris SF, Southworth DR, Agard DA. Structural Analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements. Cell. 2006 Oct 20;127(2):329-40. PMID:17055434 doi:http://dx.doi.org/10.1016/j.cell.2006.09.027
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