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New page: left|200px<br /><applet load="1gky" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gky, resolution 2.0Å" /> '''REFINED STRUCTURE OF ...
 
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[[Image:1gky.gif|left|200px]]<br /><applet load="1gky" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1gky, resolution 2.0&Aring;" />
'''REFINED STRUCTURE OF THE COMPLEX BETWEEN GUANYLATE KINASE AND ITS SUBSTRATE GMP AT 2.0 ANGSTROMS RESOLUTION'''<br />


==Overview==
==REFINED STRUCTURE OF THE COMPLEX BETWEEN GUANYLATE KINASE AND ITS SUBSTRATE GMP AT 2.0 ANGSTROMS RESOLUTION==
The crystal structure of guanylate kinase from Saccharomyces cerevisiae, complexed with its substrate GMP has been refined at a resolution of 2.0, A. The final crystallographic R-factor is 17.3% in the resolution range, 7.0 A to 2.0 A for all reflections of the 100% complete data set. The, final model has standard geometry with root-mean-square deviations of, 0.016 A in bond lengths and 3.0 in bond angles. It consists of all 186, amino acid residues, the N-terminal acetyl group, the substrate GMP, one, sulfate ion and 174 water molecules. Guanylate kinase is structurally, related to adenylate kinases and G-proteins with respect to its central, beta-sheet with connecting helices and the giant anion hole that binds, nucleoside triphosphates. These nucleotides are ATP and GTP for the, kinases and GTP for the G-proteins. The chain segment binding the, substrate GMP of guanylate kinase differs grossly from the respective part, of the adenylate kinases; it has no counterpart in the G-proteins. The, binding mode of GMP is described in detail. Probably, the observed, structure represents one of several structurally quite different, intermediate states of the catalytic cycle.
<StructureSection load='1gky' size='340' side='right'caption='[[1gky]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1gky]] 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=1GKY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GKY 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&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5GP:GUANOSINE-5-MONOPHOSPHATE'>5GP</scene>, <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1gky FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gky OCA], [https://pdbe.org/1gky PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gky RCSB], [https://www.ebi.ac.uk/pdbsum/1gky PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gky ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/KGUA_YEAST KGUA_YEAST] Essential for recycling GMP and indirectly, cGMP.
== 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/gk/1gky_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=1gky ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of guanylate kinase from Saccharomyces cerevisiae complexed with its substrate GMP has been refined at a resolution of 2.0 A. The final crystallographic R-factor is 17.3% in the resolution range 7.0 A to 2.0 A for all reflections of the 100% complete data set. The final model has standard geometry with root-mean-square deviations of 0.016 A in bond lengths and 3.0 in bond angles. It consists of all 186 amino acid residues, the N-terminal acetyl group, the substrate GMP, one sulfate ion and 174 water molecules. Guanylate kinase is structurally related to adenylate kinases and G-proteins with respect to its central beta-sheet with connecting helices and the giant anion hole that binds nucleoside triphosphates. These nucleotides are ATP and GTP for the kinases and GTP for the G-proteins. The chain segment binding the substrate GMP of guanylate kinase differs grossly from the respective part of the adenylate kinases; it has no counterpart in the G-proteins. The binding mode of GMP is described in detail. Probably, the observed structure represents one of several structurally quite different intermediate states of the catalytic cycle.


==About this Structure==
Refined structure of the complex between guanylate kinase and its substrate GMP at 2.0 A resolution.,Stehle T, Schulz GE J Mol Biol. 1992 Apr 20;224(4):1127-41. PMID:1314905<ref>PMID:1314905</ref>
1GKY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with SO4, ACE and 5GP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Guanylate_kinase Guanylate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.8 2.7.4.8] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GKY OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Refined structure of the complex between guanylate kinase and its substrate GMP at 2.0 A resolution., Stehle T, Schulz GE, J Mol Biol. 1992 Apr 20;224(4):1127-41. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1314905 1314905]
</div>
[[Category: Guanylate kinase]]
<div class="pdbe-citations 1gky" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Guanylate kinase 3D structures|Guanylate kinase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Schulz GE]]
[[Category: Schulz, G.E.]]
[[Category: Stehle T]]
[[Category: Stehle, T.]]
[[Category: 5GP]]
[[Category: ACE]]
[[Category: SO4]]
[[Category: transferase]]
 
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Retrieved from "https://proteopedia.org/1gky"