1qqm: Difference between revisions

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New page: left|200px<br /><applet load="1qqm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qqm, resolution 1.90Å" /> '''D199S MUTANT OF BOVI...
 
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[[Image:1qqm.gif|left|200px]]<br /><applet load="1qqm" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1qqm, resolution 1.90&Aring;" />
'''D199S MUTANT OF BOVINE 70 KILODALTON HEAT SHOCK PROTEIN'''<br />


==Overview==
==D199S MUTANT OF BOVINE 70 KILODALTON HEAT SHOCK PROTEIN==
ATP binding induces a conformational change in 70-kDa heat shock proteins, (Hsp70s) that facilitates release of bound polypeptides. Using the bovine, heat shock cognate protein (Hsc70) as a representative of the Hsp70, family, we have characterized the effect of mutations on the coupling, between ATP binding and the nucleotide-induced conformational change., Steady-state solution small-angle X-ray scattering and kinetic, fluorescence measurements on a 60-kDa fragment of Hsc70 show that point, mutations K71M, E175S, D199S, and D206S in the nucleotide binding cleft, impair the ability of ATP to induce a conformational change. A secondary, mutation in the peptide binding domain, E543K, "rescues" the ATP-induced, transition for three of these mutations (E175S/E543K, D199S/E543K, and, D206S/E543K) but not for K71M/E543K. Analysis of kinetics of the ATPase, cycle confirm that these effects do not result from unexpectedly rapid ATP, hydrolysis or slow ATP binding. Crystallographic structures of E175S, D199S, and D206S mutant ATPase fragment proteins show that the mutations, do not perturb the tertiary structure of the protein but do significantly, alter the protein-ligand interactions, due in part to an apparent charge, compensation effect whereby mutating a (probably) negatively charged, carboxyl group to a neutral serine displaces a K+ ion from the nucleotide, binding cleft in two out of three cases (E175S and D199S but not D206S).
<StructureSection load='1qqm' size='340' side='right'caption='[[1qqm]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1qqm]] 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=1QQM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QQM 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]] 1.9&#8491;</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=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=1qqm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qqm OCA], [https://pdbe.org/1qqm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qqm RCSB], [https://www.ebi.ac.uk/pdbsum/1qqm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qqm 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/qq/1qqm_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=1qqm ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1QQM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with MG, K, CL, PO4 and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QQM OCA].
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
 
__TOC__
==Reference==
</StructureSection>
Mapping the role of active site residues for transducing an ATP-induced conformational change in the bovine 70-kDa heat shock cognate protein., Johnson ER, McKay DB, Biochemistry. 1999 Aug 17;38(33):10823-30. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10451379 10451379]
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Johnson, E.R.]]
[[Category: Johnson ER]]
[[Category: Mckay, D.B.]]
[[Category: Mckay DB]]
[[Category: ADP]]
[[Category: CL]]
[[Category: K]]
[[Category: MG]]
[[Category: PO4]]
[[Category: atpase]]
[[Category: hydrolase (acting on acid anhydrides)]]
[[Category: molecular chaperone]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:53:54 2007''

Latest revision as of 11:16, 14 February 2024

D199S MUTANT OF BOVINE 70 KILODALTON HEAT SHOCK PROTEIND199S MUTANT OF BOVINE 70 KILODALTON HEAT SHOCK PROTEIN

Structural highlights

1qqm is a 1 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:, , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1qqm, resolution 1.90Å

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