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6vwo

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Current revision (14:40, 6 March 2024) (edit) (undo)
 
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<StructureSection load='6vwo' size='340' side='right'caption='[[6vwo]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
<StructureSection load='6vwo' size='340' side='right'caption='[[6vwo]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6vwo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VWO OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6VWO FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6vwo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VWO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VWO FirstGlance]. <br>
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</td></tr><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=GMP:GUANOSINE'>GMP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.78&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gsk, b0477, JW0466 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=GMP:GUANOSINE'>GMP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Inosine_kinase Inosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.73 2.7.1.73] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6vwo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vwo OCA], [https://pdbe.org/6vwo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vwo RCSB], [https://www.ebi.ac.uk/pdbsum/6vwo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vwo ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6vwo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vwo OCA], [http://pdbe.org/6vwo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6vwo RCSB], [http://www.ebi.ac.uk/pdbsum/6vwo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6vwo ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/INGK_ECOLI INGK_ECOLI]
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(p)ppGpp is a nucleotide messenger universally produced in bacteria following nutrient starvation. In E. coli, ppGpp inhibits purine nucleotide synthesis by targeting several different enzymes, but the physiological significance of their inhibition is unknown. Here, we report the structural basis of inhibition for one target, Gsk, the inosine-guanosine kinase. Gsk creates an unprecedented, allosteric binding pocket for ppGpp by restructuring terminal sequences, which restrains conformational dynamics necessary for catalysis. Guided by this structure, we generated a chromosomal mutation that abolishes Gsk regulation by ppGpp. This mutant strain accumulates abnormally high levels of purine nucleotides following amino-acid starvation, compromising cellular fitness. We demonstrate that this unrestricted increase in purine nucleotides is detrimental because it severely depletes pRpp and essential, pRpp-derived metabolites, including UTP, histidine, and tryptophan. Thus, our results reveal the significance of ppGpp's regulation of purine nucleotide synthesis and a critical mechanism by which E. coli coordinates biosynthetic processes during starvation.
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ppGpp Coordinates Nucleotide and Amino-Acid Synthesis in E. coli During Starvation.,Wang B, Grant RA, Laub MT Mol Cell. 2020 Oct 1;80(1):29-42.e10. doi: 10.1016/j.molcel.2020.08.005. Epub, 2020 Aug 27. PMID:32857952<ref>PMID:32857952</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6vwo" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Ecoli]]
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[[Category: Escherichia coli K-12]]
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[[Category: Inosine kinase]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Grant, R A]]
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[[Category: Grant RA]]
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[[Category: Laub, M T]]
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[[Category: Laub MT]]
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[[Category: Wang, B]]
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[[Category: Wang B]]
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[[Category: Guanosine kinase]]
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[[Category: Transferase]]
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Current revision

Crystal structure of E. coli guanosine kinase

PDB ID 6vwo

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