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| | ==Crystal structures of Leishmania mexicana pyruvate kinase (LmPYK) in complex with ATP and Oxalate== | | ==Crystal structures of Leishmania mexicana pyruvate kinase (LmPYK) in complex with ATP and Oxalate== |
| - | <StructureSection load='3hqo' size='340' side='right' caption='[[3hqo]], [[Resolution|resolution]] 3.40Å' scene=''> | + | <StructureSection load='3hqo' size='340' side='right'caption='[[3hqo]], [[Resolution|resolution]] 3.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3hqo]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Leime Leime]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HQO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HQO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3hqo]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Leishmania_mexicana Leishmania mexicana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HQO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HQO FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=OXL:OXALATE+ION'>OXL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.4Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3e0v|3e0v]], [[3e0w|3e0w]], [[1pkl|1pkl]], [[3hqn|3hqn]], [[3hqp|3hqp]], [[3hqq|3hqq]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=OXL:OXALATE+ION'>OXL</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PYK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5665 LEIME])</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=3hqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hqo OCA], [https://pdbe.org/3hqo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hqo RCSB], [https://www.ebi.ac.uk/pdbsum/3hqo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hqo ProSAT]</span></td></tr> |
| - | <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> | + | |
| - | <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=3hqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hqo OCA], [http://pdbe.org/3hqo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3hqo RCSB], [http://www.ebi.ac.uk/pdbsum/3hqo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3hqo ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/KPYK_LEIME KPYK_LEIME] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Pyruvate Kinase|Pyruvate Kinase]] | + | *[[Pyruvate kinase 3D structures|Pyruvate kinase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Leime]] | + | [[Category: Large Structures]] |
| - | [[Category: Pyruvate kinase]] | + | [[Category: Leishmania mexicana]] |
| - | [[Category: Morgan, H P]] | + | [[Category: Morgan HP]] |
| - | [[Category: Walkinshaw, M D]] | + | [[Category: Walkinshaw MD]] |
| - | [[Category: Allosteric enzyme]]
| + | |
| - | [[Category: Glycolysis]]
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| - | [[Category: Kinase]]
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| - | [[Category: Magnesium]]
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| - | [[Category: Metal-binding]]
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| - | [[Category: Pyruvate]]
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| - | [[Category: R-state enzyme]]
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| - | [[Category: Tim barrel]]
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| - | [[Category: Transferase]]
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| Structural highlights
Function
KPYK_LEIME
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Allosteric regulation provides a rate management system for enzymes involved in many cellular processes. Ligand-controlled regulation is easily recognizable, but the underlying molecular mechanisms have remained elusive. We have obtained the first complete series of allosteric structures, in all possible ligated states, for the tetrameric enzyme, pyruvate kinase, from Leishmania mexicana. The transition between inactive T-state and active R-state is accompanied by a simple symmetrical 6 degrees rigid body rocking motion of the A- and C-domain cores in each of the four subunits. However, formation of the R-state in this way is only part of the mechanism; eight essential salt bridge locks that form across the C-C interface provide tetramer rigidity with a coupled 7-fold increase in rate. The results presented here illustrate how conformational changes coupled with effector binding correlate with loss of flexibility and increase in thermal stability providing a general mechanism for allosteric control.
Allosteric mechanism of pyruvate kinase from Leishmania mexicana uses a rock and lock model.,Morgan HP, McNae IW, Nowicki MW, Hannaert V, Michels PA, Fothergill-Gilmore LA, Walkinshaw MD J Biol Chem. 2010 Apr 23;285(17):12892-8. Epub 2010 Feb 1. PMID:20123988[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Morgan HP, McNae IW, Nowicki MW, Hannaert V, Michels PA, Fothergill-Gilmore LA, Walkinshaw MD. Allosteric mechanism of pyruvate kinase from Leishmania mexicana uses a rock and lock model. J Biol Chem. 2010 Apr 23;285(17):12892-8. Epub 2010 Feb 1. PMID:20123988 doi:10.1074/jbc.M109.079905
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