2qwo: Difference between revisions

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[[Image:2qwo.jpg|left|200px]]
[[Image:2qwo.jpg|left|200px]]


{{Structure
<!--
|PDB= 2qwo |SIZE=350|CAPTION= <scene name='initialview01'>2qwo</scene>, resolution 1.700&Aring;
The line below this paragraph, containing "STRUCTURE_2qwo", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
|LIGAND= <scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=ADP:ADENOSINE-5&#39;-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </span>
or leave the SCENE parameter empty for the default display.
|GENE= HSPA8, HSC70 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus]), DNAJC6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus])
-->
|DOMAIN=
{{STRUCTURE_2qwo|  PDB=2qwo |  SCENE= }}  
|RELATEDENTRY=[[2qwl|2QWL]], [[2qwm|2QWM]], [[2qwn|2QWN]], [[2qwp|2QWP]], [[2qwq|2QWQ]], [[2qwr|2QWR]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qwo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qwo OCA], [http://www.ebi.ac.uk/pdbsum/2qwo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2qwo RCSB]</span>
}}


'''Crystal structure of disulfide-bond-crosslinked complex of bovine hsc70 (1-394aa)R171C and bovine Auxilin (810-910aa)D876C in the ADP*Pi form #1'''
'''Crystal structure of disulfide-bond-crosslinked complex of bovine hsc70 (1-394aa)R171C and bovine Auxilin (810-910aa)D876C in the ADP*Pi form #1'''
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[[Category: Taylor, A B.]]
[[Category: Taylor, A B.]]
[[Category: Wang, L.]]
[[Category: Wang, L.]]
[[Category: atp-binding]]
[[Category: Atp-binding]]
[[Category: chaperone-cochaperone complex]]
[[Category: Chaperone-cochaperone complex]]
[[Category: cytoplasm]]
[[Category: Cytoplasm]]
[[Category: hydrolase]]
[[Category: Hydrolase]]
[[Category: nucleotide-binding]]
[[Category: Nucleotide-binding]]
[[Category: nucleus]]
[[Category: Nucleus]]
[[Category: phosphorylation]]
[[Category: Phosphorylation]]
[[Category: protein phosphatase]]
[[Category: Protein phosphatase]]
[[Category: sh3-binding]]
[[Category: Sh3-binding]]
[[Category: stress response]]
[[Category: Stress response]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 15:49:40 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:54:13 2008''

Revision as of 15:49, 4 May 2008

File:2qwo.jpg

Template:STRUCTURE 2qwo

Crystal structure of disulfide-bond-crosslinked complex of bovine hsc70 (1-394aa)R171C and bovine Auxilin (810-910aa)D876C in the ADP*Pi form #1


OverviewOverview

The many protein processing reactions of the ATP-hydrolyzing Hsp70s are regulated by J cochaperones, which contain J domains that stimulate Hsp70 ATPase activity and accessory domains that present protein substrates to Hsp70s. We report the structure of a J domain complexed with a J responsive portion of a mammalian Hsp70. The J domain activates ATPase activity by directing the linker that connects the Hsp70 nucleotide binding domain (NBD) and substrate binding domain (SBD) toward a hydrophobic patch on the NBD surface. Binding of the J domain to Hsp70 displaces the SBD from the NBD, which may allow the SBD flexibility to capture diverse substrates. Unlike prokaryotic Hsp70, the SBD and NBD of the mammalian chaperone interact in the ADP state. Thus, although both nucleotides and J cochaperones modulate Hsp70 NBD:linker and NBD:SBD interactions, the intrinsic persistence of those interactions differs in different Hsp70s and this may optimize their activities for different cellular roles.

About this StructureAbout this Structure

2QWO is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis of J cochaperone binding and regulation of Hsp70., Jiang J, Maes EG, Taylor AB, Wang L, Hinck AP, Lafer EM, Sousa R, Mol Cell. 2007 Nov 9;28(3):422-33. PMID:17996706 Page seeded by OCA on Sun May 4 15:49:40 2008

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