1yuw: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
New page: left|200px<br /><applet load="1yuw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yuw, resolution 2.600Å" /> '''crystal structure o...
 
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
No edit summary
 
(15 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1yuw.gif|left|200px]]<br /><applet load="1yuw" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1yuw, resolution 2.600&Aring;" />
'''crystal structure of bovine hsc70(aa1-554)E213A/D214A mutant'''<br />


==Overview==
==crystal structure of bovine hsc70(aa1-554)E213A/D214A mutant==
Hsp70 family proteins are highly conserved chaperones involved in protein, folding, degradation, targeting and translocation, and protein complex, remodeling. They are comprised of an N-terminal nucleotide binding domain, (NBD) and a C-terminal protein substrate binding domain (SBD). ATP binding, to the NBD alters SBD conformation and substrate binding kinetics, but an, understanding of the mechanism of interdomain communication has been, hampered by the lack of a crystal structure of an intact chaperone. We, report here the 2.6 angstroms structure of a functionally intact bovine, Hsc70 (bHsc70) and a mutational analysis of the observed interdomain, interface and the immediately adjacent interdomain linker. This analysis, identifies interdomain interactions critical for chaperone function and, supports an allosteric mechanism in which the interdomain linker invades, and disrupts the interdomain interface when ATP binds.
<StructureSection load='1yuw' size='340' side='right'caption='[[1yuw]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1yuw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YUW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YUW FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</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=1yuw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yuw OCA], [https://pdbe.org/1yuw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yuw RCSB], [https://www.ebi.ac.uk/pdbsum/1yuw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yuw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HSP7C_BOVIN HSP7C_BOVIN] 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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yu/1yuw_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </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/main_output.php?pdb_ID=1yuw ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1YUW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YUW OCA].
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
 
__TOC__
==Reference==
</StructureSection>
Structural basis of interdomain communication in the Hsc70 chaperone., Jiang J, Prasad K, Lafer EM, Sousa R, Mol Cell. 2005 Nov 23;20(4):513-24. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16307916 16307916]
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Jiang, J.]]
[[Category: Jiang J]]
[[Category: Lafer, E.M.]]
[[Category: Lafer EM]]
[[Category: Prasad, K.]]
[[Category: Prasad K]]
[[Category: Sousa, R.]]
[[Category: Sousa R]]
[[Category: chaperone]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:03:57 2007''
Retrieved from "https://proteopedia.org/1yuw"