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6znt
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 6znt is ON HOLD Authors: Lovering, A.L., Harding, C.J. Description: MaeB PTA domain, acetyl-CoA bound form Category: Unreleased Structures [[Ca...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==MaeB PTA domain, acetyl-CoA bound form== | |
| + | <StructureSection load='6znt' size='340' side='right'caption='[[6znt]], [[Resolution|resolution]] 1.96Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6znt]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Bdellovibrio_bacteriovorus_HD100 Bdellovibrio bacteriovorus HD100]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZNT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZNT 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]] 1.96Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=6znt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6znt OCA], [https://pdbe.org/6znt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6znt RCSB], [https://www.ebi.ac.uk/pdbsum/6znt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6znt ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q6MM15_BDEBA Q6MM15_BDEBA] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Bacterial hybrid malic enzymes (MaeB grouping, multidomain) catalyse the transformation of malate to pyruvate, and are a major contributor to cellular reducing power and carbon flux. Distinct from other malic enzyme subtypes, the hybrid enzymes are regulated by acetyl-CoA, a molecular indicator of the metabolic state of the cell. Here we solve the structure of a MaeB protein, which reveals hybrid enzymes use the appended phosphotransacetylase (PTA) domain to form a hexameric sensor that communicates acetyl-CoA occupancy to the malic enzyme active site, 60 A away. We demonstrate that allostery is governed by a large-scale rearrangement that rotates the catalytic subunits 70 degrees between the two states, identifying MaeB as a new model enzyme for the study of ligand-induced conformational change. Our work provides the mechanistic basis for metabolic control of hybrid malic enzymes, and identifies inhibition-insensitive variants that may find utility in synthetic biology. | ||
| - | + | A rotary mechanism for allostery in bacterial hybrid malic enzymes.,Harding CJ, Cadby IT, Moynihan PJ, Lovering AL Nat Commun. 2021 Feb 23;12(1):1228. doi: 10.1038/s41467-021-21528-2. PMID:33623032<ref>PMID:33623032</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Harding | + | <div class="pdbe-citations 6znt" style="background-color:#fffaf0;"></div> |
| - | [[Category: Lovering | + | |
| + | ==See Also== | ||
| + | *[[Malate Dehydrogenase 3D structures|Malate Dehydrogenase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bdellovibrio bacteriovorus HD100]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Harding CJ]] | ||
| + | [[Category: Lovering AL]] | ||
Current revision
MaeB PTA domain, acetyl-CoA bound form
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