2bup: Difference between revisions

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-[[Image:2bup.jpg|left|200px]]<br /><applet load="2bup" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="2bup, resolution 1.70&Aring;" />
-'''T13G MUTANT OF THE ATPASE FRAGMENT OF BOVINE HSC70'''<br />
-==Overview==
+==T13G Mutant of the ATPASE fragment of Bovine HSC70==
-The mechanism by which ATP binding transduces a conformational change in, 70-kDa heat shock proteins that results in release of bound peptides, remains obscure. Wei and Hendershot demonstrated that mutating Thr37 of, hamster BiP to glycine impeded the ATP-induced conformational change, as, monitored by proteolysis [(1995) J. Biol. Chem. 270, 26670-26676]. We have, mutated the equivalent resitude of the bovine heat shock cognate protein, (Hsc70), Thr13, to serine, valine, and glycine. Solution small-angle X-ray, scattering experiments on a 60-kDa fragment of Hsc70 show that ATP binding, induces a conformational change in the T13S mutant but not the T13V or, T13G mutants. The kinetics of ATP-induced tryptophan fluorescence, intensity changes in the 60-kDa proteins is biphasic for the T13S mutant, but monophasic for T13V or T13G, consistent with a conformational change, following initial ATP binding in the T13S mutant but not the other two., Crystallographic structures of the ATPase fragments of the T13S and T13G, mutants at 1.7 A resolution show that the mutations do not disrupt the ATP, binding site and that the serine hydroxyl mimics the threonine hydroxyl in, the wild-type structure. We conclude that the hydroxyl of Thr13 is, essential for coupling ATP binding to a conformational change in Hsc70., Molecular modeling suggests this may result from the threonine hydroxyl, hydrogen-bonding to a gamma-phosphate oxygen of ATP, thereby inducing a, structural shift within the ATPase domain that couples to its interactions, with the peptide binding domain.
+<StructureSection load='2bup' size='340' side='right'caption='[[2bup]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2bup]] 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=2BUP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BUP 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]] 1.7&#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=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</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=2bup FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bup OCA], [https://pdbe.org/2bup PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bup RCSB], [https://www.ebi.ac.uk/pdbsum/2bup PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bup 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/bu/2bup_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=2bup ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-BUP 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 PO4, MG, K, CL, ADP and ATP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BUP OCA].
+*[[Heat Shock Protein structures|Heat Shock Protein structures]]
+__TOC__
-==Reference==
+</StructureSection>
-The hydroxyl of threonine 13 of the bovine 70-kDa heat shock cognate protein is essential for transducing the ATP-induced conformational change., Sousa MC, McKay DB, Biochemistry. 1998 Nov 3;37(44):15392-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9799500 9799500]
 [[Category: Bos taurus]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Mckay, D.B.]]
+[[Category: Mckay DB]]
-[[Category: Sousa, M.C.]]
+[[Category: Sousa MC]]
-[[Category: ADP]]
-[[Category: ATP]]
-[[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 08:55:35 2007''