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1ngj

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STRUCTURAL BASIS OF THE 70-KILODALTON HEAT SHOCK COGNATE PROTEIN ATP HYDROLYTIC ACTIVITY, II. STRUCTURE OF THE ACTIVE SITE WITH ADP OR ATP BOUND TO WILD TYPE AND MUTANT ATPASE FRAGMENT

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Retrieved from "http://52.214.119.220/wiki/index.php/1ngj"

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-[[Image:1ngj.jpg|left|200px]]<br /><applet load="1ngj" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1ngj, resolution 2.10&Aring;" />
-'''STRUCTURAL BASIS OF THE 70-KILODALTON HEAT SHOCK COGNATE PROTEIN ATP HYDROLYTIC ACTIVITY, II. STRUCTURE OF THE ACTIVE SITE WITH ADP OR ATP BOUND TO WILD TYPE AND MUTANT ATPASE FRAGMENT'''<br />
-==Overview==
+==STRUCTURAL BASIS OF THE 70-KILODALTON HEAT SHOCK COGNATE PROTEIN ATP HYDROLYTIC ACTIVITY, II. STRUCTURE OF THE ACTIVE SITE WITH ADP OR ATP BOUND TO WILD TYPE AND MUTANT ATPASE FRAGMENT==
-The ATPase fragment of the bovine 70-kDa heat shock cognate protein is an, attractive construct in which to study its mechanism of ATP hydrolysis., The three-dimensional structure suggests several residues that might, participate in the ATPase reaction. Four acidic residues (Asp-10, Glu-175, Asp-199, and Asp-206) have been individually mutated to both the cognate, amine (asparagine/glutamine) and to serine, and the effects of the, mutations on the kinetics of the ATPase activity (Wilbanks, S. M., DeLuca-Flaherty, C., and McKay, D. B. (1994) J. Biol. Chem. 269, 12893-12898) and the structure of the mutant ATPase fragments have been, determined, typically to approximately 2.4 A resolution. Additionally, the, structures of the wild type protein complexed with MgADP and Pi, MgAMPPNP, (5'-adenylyl-beta, gamma-imidodiphosphate) and CaAMPPNP have been refined, to 2.1, 2.4, and 2.4 A, respectively. Combined, these structures provide, models for the prehydrolysis, MgATP-bound state and the post-hydrolysis, MgADP-bound state of the ATPase fragment. These models suggest a pathway, for the hydrolytic reaction in which 1) the gamma phosphate of bound ATP, reorients to form a beta, gamma-bidentate phosphate complex with the Mg2+, ion, allowing 2) in-line nucleophilic attack on the gamma phosphate by a, H2O molecule or OH- ion, with 3) subsequent release of inorganic, phosphate.
+<StructureSection load='1ngj' size='340' side='right'caption='[[1ngj]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1ngj]] 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=1NGJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NGJ 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]] 2.1&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=1ngj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ngj OCA], [https://pdbe.org/1ngj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ngj RCSB], [https://www.ebi.ac.uk/pdbsum/1ngj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ngj 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/ng/1ngj_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=1ngj ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-NGJ 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 and ANP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Adenosinetriphosphatase Adenosinetriphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.3 3.6.1.3] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NGJ OCA].
+*[[Heat Shock Protein structures|Heat Shock Protein structures]]
+__TOC__
-==Reference==
+</StructureSection>
-Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. II. Structure of the active site with ADP or ATP bound to wild type and mutant ATPase fragment., Flaherty KM, Wilbanks SM, DeLuca-Flaherty C, McKay DB, J Biol Chem. 1994 Apr 29;269(17):12899-907. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8175707 8175707]
-[[Category: Adenosinetriphosphatase]]
 [[Category: Bos taurus]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Deluca-Flaherty, C.]]
+[[Category: Deluca-Flaherty C]]
-[[Category: Flaherty, K.M.]]
+[[Category: Flaherty KM]]
-[[Category: Mckay, D.B.]]
+[[Category: Mckay DB]]
-[[Category: Wilbanks, S.M.]]
+[[Category: Wilbanks SM]]
-[[Category: ANP]]
-[[Category: MG]]
-[[Category: hydrolase(acting on acid anhydrides)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:14:32 2007''

1ngj

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Current revision

STRUCTURAL BASIS OF THE 70-KILODALTON HEAT SHOCK COGNATE PROTEIN ATP HYDROLYTIC ACTIVITY, II. STRUCTURE OF THE ACTIVE SITE WITH ADP OR ATP BOUND TO WILD TYPE AND MUTANT ATPASE FRAGMENT

Structural highlights

Function

Evolutionary Conservation

See Also

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