1fot: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
New page: left|200px<br /><applet load="1fot" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fot, resolution 2.80Å" /> '''STRUCTURE OF THE UNL...
 
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
 
(16 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1fot.gif|left|200px]]<br /><applet load="1fot" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1fot, resolution 2.80&Aring;" />
'''STRUCTURE OF THE UNLIGANDED CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT FROM SACCHAROMYCES CEREVISIAE'''<br />


==Overview==
==STRUCTURE OF THE UNLIGANDED CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT FROM SACCHAROMYCES CEREVISIAE==
The structure of TPK1delta, a truncated variant of the cAMP-dependent, protein kinase catalytic subunit from Saccharomyces cerevisiae, was, determined in an unliganded state at 2.8 A resolution and refined to a, crystallographic R-factor of 19.4%. Comparison of this structure to that, of its fully liganded mammalian homolog revealed a highly conserved, protein fold comprised of two globular lobes. Within each lobe, root mean, square deviations in Calpha positions averaged approximately equals 0.9 A., In addition, a phosphothreonine residue was found in the C-terminal domain, of each enzyme. Further comparison of the two structures suggests that a, trio of conformational changes accompanies ligand-binding. The first, consists of a 14.7 degrees rigid-body rotation of one lobe relative to the, other and results in closure of the active site cleft. The second affects, only the glycine-rich nucleotide binding loop, which moves approximately, equals 3 A to further close the active site and traps the nucleotide, substrate. The third is localized to a C-terminal segment that makes, direct contact with ligands and the ligand-binding cleft. In addition to, resolving the conformation of unliganded enzyme, the model shows that the, salient features of the cAMP-dependent protein kinase are conserved over, long evolutionary distances.
<StructureSection load='1fot' size='340' side='right'caption='[[1fot]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1fot]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FOT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FOT 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]] 2.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</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=1fot FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fot OCA], [https://pdbe.org/1fot PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fot RCSB], [https://www.ebi.ac.uk/pdbsum/1fot PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fot ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/KAPA_YEAST KAPA_YEAST]
== 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/fo/1fot_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1fot ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The structure of TPK1delta, a truncated variant of the cAMP-dependent protein kinase catalytic subunit from Saccharomyces cerevisiae, was determined in an unliganded state at 2.8 A resolution and refined to a crystallographic R-factor of 19.4%. Comparison of this structure to that of its fully liganded mammalian homolog revealed a highly conserved protein fold comprised of two globular lobes. Within each lobe, root mean square deviations in Calpha positions averaged approximately equals 0.9 A. In addition, a phosphothreonine residue was found in the C-terminal domain of each enzyme. Further comparison of the two structures suggests that a trio of conformational changes accompanies ligand-binding. The first consists of a 14.7 degrees rigid-body rotation of one lobe relative to the other and results in closure of the active site cleft. The second affects only the glycine-rich nucleotide binding loop, which moves approximately equals 3 A to further close the active site and traps the nucleotide substrate. The third is localized to a C-terminal segment that makes direct contact with ligands and the ligand-binding cleft. In addition to resolving the conformation of unliganded enzyme, the model shows that the salient features of the cAMP-dependent protein kinase are conserved over long evolutionary distances.


==About this Structure==
Structure of the unliganded cAMP-dependent protein kinase catalytic subunit from Saccharomyces cerevisiae.,Mashhoon N, Carmel G, Pflugrath JW, Kuret J Arch Biochem Biophys. 2001 Mar 1;387(1):11-9. PMID:11368172<ref>PMID:11368172</ref>
1FOT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Active as [http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FOT OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Structure of the unliganded cAMP-dependent protein kinase catalytic subunit from Saccharomyces cerevisiae., Mashhoon N, Carmel G, Pflugrath JW, Kuret J, Arch Biochem Biophys. 2001 Mar 1;387(1):11-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11368172 11368172]
</div>
[[Category: Non-specific serine/threonine protein kinase]]
<div class="pdbe-citations 1fot" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[CAMP-dependent protein kinase 3D structures|CAMP-dependent protein kinase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Carmel G]]
[[Category: Carmel, G.]]
[[Category: Kuret J]]
[[Category: Kuret, J.]]
[[Category: Mashhoon N]]
[[Category: Mashhoon, N.]]
[[Category: Pflugrath JW]]
[[Category: Pflugrath, J.W.]]
[[Category: camp-dependent protein kinase]]
[[Category: open conformation]]
[[Category: protein kinase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:06:06 2007''
Retrieved from "https://proteopedia.org/1fot"