8q1f: Difference between revisions
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==D10N,P146A variant of beta-phosphoglucomutase from Lactococcus lactis in complex with native beta-glucose 1,6-bisphosphate intermediate== | |||
<StructureSection load='8q1f' size='340' side='right'caption='[[8q1f]], [[Resolution|resolution]] 1.01Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8q1f]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactococcus_lactis_subsp._lactis_Il1403 Lactococcus lactis subsp. lactis Il1403]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8Q1F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8Q1F 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]] 1.01Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B16:1,6-DI-O-PHOSPHONO-BETA-D-GLUCOPYRANOSE'>B16</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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=8q1f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8q1f OCA], [https://pdbe.org/8q1f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8q1f RCSB], [https://www.ebi.ac.uk/pdbsum/8q1f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8q1f ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A0A7T4I1_LACLL A0A0A7T4I1_LACLL] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Metabolic regulation occurs through precise control of enzyme activity. Allomorphy is a post-translational fine control mechanism where the catalytic rate is governed by a conformational switch that shifts the enzyme population between forms with different activities. beta-Phosphoglucomutase (betaPGM) uses allomorphy in the catalysis of isomerisation of beta-glucose 1-phosphate to glucose 6-phosphate via beta-glucose 1,6-bisphosphate. Herein, we describe structural and biophysical approaches to reveal its allomorphic regulatory mechanism. Binding of the full allomorphic activator beta-glucose 1,6-bisphosphate stimulates enzyme closure, progressing through NAC I and NAC III conformers. Prior to phosphoryl transfer, loops positioned on the cap and core domains are brought into close proximity, modulating the environment of a key proline residue. Hence accelerated isomerisation, likely via a twisted anti/C4-endo transition state, leads to the rapid predominance of active cis-P betaPGM. In contrast, binding of the partial allomorphic activator fructose 1,6-bisphosphate arrests betaPGM at a NAC I conformation and phosphoryl transfer to both cis-P betaPGM and trans-P betaPGM occurs slowly. Thus, allomorphy allows a rapid response to changes in food supply while not otherwise impacting substantially on levels of important metabolites. | |||
Peri active site catalysis of proline isomerisation is the molecular basis of allomorphy in beta-phosphoglucomutase.,Cruz-Navarrete FA, Baxter NJ, Flinders AJ, Buzoianu A, Cliff MJ, Baker PJ, Waltho JP Commun Biol. 2024 Jul 27;7(1):909. doi: 10.1038/s42003-024-06577-9. PMID:39068257<ref>PMID:39068257</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8q1f" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Lactococcus lactis subsp. lactis Il1403]] | |||
[[Category: Large Structures]] | |||
[[Category: Baker PJ]] | |||
[[Category: Baxter NJ]] | |||
[[Category: Buzoianu A]] | |||
[[Category: Cliff MJ]] | |||
[[Category: Cruz-Navarrete FA]] | |||
[[Category: Flinders AJ]] | |||
[[Category: Waltho JP]] | |||
Latest revision as of 08:39, 7 August 2024
D10N,P146A variant of beta-phosphoglucomutase from Lactococcus lactis in complex with native beta-glucose 1,6-bisphosphate intermediateD10N,P146A variant of beta-phosphoglucomutase from Lactococcus lactis in complex with native beta-glucose 1,6-bisphosphate intermediate
Structural highlights
FunctionPublication Abstract from PubMedMetabolic regulation occurs through precise control of enzyme activity. Allomorphy is a post-translational fine control mechanism where the catalytic rate is governed by a conformational switch that shifts the enzyme population between forms with different activities. beta-Phosphoglucomutase (betaPGM) uses allomorphy in the catalysis of isomerisation of beta-glucose 1-phosphate to glucose 6-phosphate via beta-glucose 1,6-bisphosphate. Herein, we describe structural and biophysical approaches to reveal its allomorphic regulatory mechanism. Binding of the full allomorphic activator beta-glucose 1,6-bisphosphate stimulates enzyme closure, progressing through NAC I and NAC III conformers. Prior to phosphoryl transfer, loops positioned on the cap and core domains are brought into close proximity, modulating the environment of a key proline residue. Hence accelerated isomerisation, likely via a twisted anti/C4-endo transition state, leads to the rapid predominance of active cis-P betaPGM. In contrast, binding of the partial allomorphic activator fructose 1,6-bisphosphate arrests betaPGM at a NAC I conformation and phosphoryl transfer to both cis-P betaPGM and trans-P betaPGM occurs slowly. Thus, allomorphy allows a rapid response to changes in food supply while not otherwise impacting substantially on levels of important metabolites. Peri active site catalysis of proline isomerisation is the molecular basis of allomorphy in beta-phosphoglucomutase.,Cruz-Navarrete FA, Baxter NJ, Flinders AJ, Buzoianu A, Cliff MJ, Baker PJ, Waltho JP Commun Biol. 2024 Jul 27;7(1):909. doi: 10.1038/s42003-024-06577-9. PMID:39068257[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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