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5wrp

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==T-state crystal structure of pyruvate kinase from Mycobacterium tuberculosis==
==T-state crystal structure of pyruvate kinase from Mycobacterium tuberculosis==
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<StructureSection load='5wrp' size='340' side='right' caption='[[5wrp]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
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<StructureSection load='5wrp' size='340' side='right'caption='[[5wrp]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5wrp]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WRP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WRP FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5wrp]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WRP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WRP FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 2.85&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ws8|5ws8]], [[5ws9|5ws9]], [[5wsa|5wsa]], [[5wsb|5wsb]], [[5wsc|5wsc]]</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=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pyk, pykA, Rv1617, MTCY01B2.09 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</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=5wrp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wrp OCA], [https://pdbe.org/5wrp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wrp RCSB], [https://www.ebi.ac.uk/pdbsum/5wrp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wrp ProSAT]</span></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/Pyruvate_kinase Pyruvate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.40 2.7.1.40] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5wrp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wrp OCA], [http://pdbe.org/5wrp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wrp RCSB], [http://www.ebi.ac.uk/pdbsum/5wrp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wrp 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/KPYK_MYCTU KPYK_MYCTU]
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Pyruvate kinase (PYK) is an essential glycolytic enzyme that controls glycolytic flux and is critical for ATP production in all organisms, with tight regulation by multiple metabolites. Yet the allosteric mechanisms governing PYK activity in bacterial pathogens are poorly understood. Here we report biochemical, structural and metabolomic evidence that Mycobacterium tuberculosis (Mtb) PYK uses AMP and glucose-6-phosphate (G6P) as synergistic allosteric activators that function as a molecular "OR logic gate" to tightly regulate energy and glucose metabolism. G6P was found to bind to a previously unknown site adjacent to the canonical site for AMP. Kinetic data and structural network analysis further show that AMP and G6P work synergistically as allosteric activators. Importantly, metabolome profiling in the Mtb surrogate, Mycobacterium bovis BCG, reveals significant changes in AMP and G6P levels during nutrient deprivation, which provides insights into how a PYK OR gate would function during the stress of Mtb infection.
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Allosteric pyruvate kinase-based "logic gate" synergistically senses energy and sugar levels in Mycobacterium tuberculosis.,Zhong W, Cui L, Goh BC, Cai Q, Ho P, Chionh YH, Yuan M, Sahili AE, Fothergill-Gilmore LA, Walkinshaw MD, Lescar J, Dedon PC Nat Commun. 2017 Dec 7;8(1):1986. doi: 10.1038/s41467-017-02086-y. PMID:29215013<ref>PMID:29215013</ref>
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==See Also==
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*[[Pyruvate kinase 3D structures|Pyruvate kinase 3D structures]]
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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 5wrp" 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: Myctu]]
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[[Category: Large Structures]]
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[[Category: Pyruvate kinase]]
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[[Category: Mycobacterium tuberculosis H37Rv]]
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[[Category: Cai, Q]]
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[[Category: Cai Q]]
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[[Category: Dedon, P C]]
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[[Category: Dedon PC]]
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[[Category: Lescar, J]]
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[[Category: El Sahili A]]
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[[Category: Sahili, A El]]
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[[Category: Lescar J]]
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[[Category: Zhong, W]]
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[[Category: Zhong W]]
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[[Category: Allostery]]
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[[Category: Glycolysis]]
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[[Category: Phospho transferase]]
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[[Category: Synergism]]
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[[Category: Tetramer]]
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[[Category: Transferase]]
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Current revision

T-state crystal structure of pyruvate kinase from Mycobacterium tuberculosis

PDB ID 5wrp

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