View source for 4qrh


==Molecular mechanism and evolution of guanylate kinase regulation by (p)ppGpp==
<StructureSection load='4qrh' size='340' side='right'caption='[[4qrh]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4qrh]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_USA300-ISMMS1 Staphylococcus aureus USA300-ISMMS1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QRH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QRH 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]] 1.65&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0O2:GUANOSINE+5-(TETRAHYDROGEN+TRIPHOSPHATE)+3-(TRIHYDROGEN+DIPHOSPHATE)'>0O2</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=4qrh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qrh OCA], [https://pdbe.org/4qrh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qrh RCSB], [https://www.ebi.ac.uk/pdbsum/4qrh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qrh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0J9X1Z9_STAAU A0A0J9X1Z9_STAAU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The nucleotide (p)ppGpp mediates bacterial stress responses, but its targets and underlying mechanisms of action vary among bacterial species and remain incompletely understood. Here, we characterize the molecular interaction between (p)ppGpp and guanylate kinase (GMK), revealing the importance of this interaction in adaptation to starvation. Combining structural and kinetic analyses, we show that (p)ppGpp binds the GMK active site and competitively inhibits the enzyme. The (p)ppGpp-GMK interaction prevents the conversion of GMP to GDP, resulting in GMP accumulation upon amino acid downshift. Abolishing this interaction leads to excess (p)ppGpp and defective adaptation to amino acid starvation. A survey of GMKs from phylogenetically diverse bacteria shows that the (p)ppGpp-GMK interaction is conserved in members of Firmicutes, Actinobacteria, and Deinococcus-Thermus, but not in Proteobacteria, where (p)ppGpp regulates RNA polymerase (RNAP). We propose that GMK is an ancestral (p)ppGpp target and RNAP evolved more recently as a direct target in Proteobacteria.

Molecular Mechanism and Evolution of Guanylate Kinase Regulation by (p)ppGpp.,Liu K, Myers AR, Pisithkul T, Claas KR, Satyshur KA, Amador-Noguez D, Keck JL, Wang JD Mol Cell. 2015 Feb 19;57(4):735-49. doi: 10.1016/j.molcel.2014.12.037. Epub 2015 , Feb 5. PMID:25661490<ref>PMID:25661490</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4qrh" style="background-color:#fffaf0;"></div>

==See Also==
*[[Guanylate kinase 3D structures|Guanylate kinase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Staphylococcus aureus USA300-ISMMS1]]
[[Category: Keck JL]]
[[Category: Krasny K]]
[[Category: Liu K]]
[[Category: Myers AR]]
[[Category: Satyshur KA]]
[[Category: Wnag JD]]