2gq0
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= | ||
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Non-chaperonin_molecular_chaperone_ATPase Non-chaperonin molecular chaperone ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.10 3.6.4.10] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-chaperonin_molecular_chaperone_ATPase Non-chaperonin molecular chaperone ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.10 3.6.4.10] </span> |
|GENE= htpG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= htpG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1sf8|1SF8]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2gq0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gq0 OCA], [http://www.ebi.ac.uk/pdbsum/2gq0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2gq0 RCSB]</span> | ||
}} | }} | ||
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[[Category: molecular chaperone]] | [[Category: molecular chaperone]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:19:57 2008'' |
Revision as of 00:19, 31 March 2008
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| , resolution 1.90Å | |||||||
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| Gene: | htpG (Escherichia coli) | ||||||
| Activity: | Non-chaperonin molecular chaperone ATPase, with EC number 3.6.4.10 | ||||||
| Related: | 1SF8
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of the Middle Domain of HtpG, the E. coli Hsp90
Overview
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.
About this Structure
2GQ0 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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
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