1ats: Difference between revisions

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[[Image:1ats.png|left|200px]]


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==THREONINE 204 OF THE CHAPERONE PROTEIN HSC70 INFLUENCES THE STRUCTURE OF THE ACTIVE SITE BUT IS NOT ESSENTIAL FOR ATP HYDROLYSIS==
The line below this paragraph, containing "STRUCTURE_1ats", creates the "Structure Box" on the page.
<StructureSection load='1ats' size='340' side='right'caption='[[1ats]], [[Resolution|resolution]] 2.43&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1ats]] 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=1ATS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ATS FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.43&#8491;</td></tr>
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<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=MG:MAGNESIUM+ION'>MG</scene></td></tr>
{{STRUCTURE_1ats| PDB=1ats |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ats FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ats OCA], [https://pdbe.org/1ats PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ats RCSB], [https://www.ebi.ac.uk/pdbsum/1ats PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ats 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/at/1ats_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=1ats ConSurf].
<div style="clear:both"></div>


===THREONINE 204 OF THE CHAPERONE PROTEIN HSC70 INFLUENCES THE STRUCTURE OF THE ACTIVE SITE BUT IS NOT ESSENTIAL FOR ATP HYDROLYSIS===
==See Also==
 
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
 
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</StructureSection>
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{{ABSTRACT_PUBMED_8226982}}
 
==About this Structure==
1ATS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ATS OCA].
 
==Reference==
Threonine 204 of the chaperone protein Hsc70 influences the structure of the active site, but is not essential for ATP hydrolysis., O'Brien MC, McKay DB, J Biol Chem. 1993 Nov 15;268(32):24323-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8226982 8226982]
[[Category: Adenosinetriphosphatase]]
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Brien, M C.O.]]
[[Category: Mckay DB]]
[[Category: Mckay, D B.]]
[[Category: O'Brien MC]]
[[Category: Chaperone protein]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:34:46 2008''

Latest revision as of 09:33, 7 February 2024

THREONINE 204 OF THE CHAPERONE PROTEIN HSC70 INFLUENCES THE STRUCTURE OF THE ACTIVE SITE BUT IS NOT ESSENTIAL FOR ATP HYDROLYSISTHREONINE 204 OF THE CHAPERONE PROTEIN HSC70 INFLUENCES THE STRUCTURE OF THE ACTIVE SITE BUT IS NOT ESSENTIAL FOR ATP HYDROLYSIS

Structural highlights

1ats 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 2.43Å
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

1ats, resolution 2.43Å

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