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6znu
From Proteopedia
(Difference between revisions)
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==MaeB PTA domain E544R mutant== | ==MaeB PTA domain E544R mutant== | ||
| - | <StructureSection load='6znu' size='340' side='right'caption='[[6znu]]' scene=''> | + | <StructureSection load='6znu' size='340' side='right'caption='[[6znu]], [[Resolution|resolution]] 2.33Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZNU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZNU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6znu]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Bdeba Bdeba]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZNU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZNU FirstGlance]. <br> |
| - | </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=6znu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6znu OCA], [https://pdbe.org/6znu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6znu RCSB], [https://www.ebi.ac.uk/pdbsum/6znu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6znu ProSAT]</span></td></tr> | + | </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=CL:CHLORIDE+ION'>CL</scene></td></tr> |
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[6zn4|6zn4]], [[6zn7|6zn7]], [[6znt|6znt]], [[6zn9|6zn9]], [[6znr|6znr]], [[6zne|6zne]], [[6znk|6znk]], [[6zng|6zng]], [[6znj|6znj]]</div></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mdh, Bd1833 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=264462 BDEBA])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Malate_dehydrogenase_(oxaloacetate-decarboxylating)_(NADP(+)) Malate dehydrogenase (oxaloacetate-decarboxylating) (NADP(+))], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.40 1.1.1.40] </span></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=6znu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6znu OCA], [https://pdbe.org/6znu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6znu RCSB], [https://www.ebi.ac.uk/pdbsum/6znu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6znu ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <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> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6znu" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Bdeba]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Harding | + | [[Category: Harding, C J]] |
| - | [[Category: Lovering | + | [[Category: Lovering, A L]] |
| + | [[Category: Malic enzyme]] | ||
| + | [[Category: Oxidoreductase]] | ||
Revision as of 06:56, 17 March 2021
MaeB PTA domain E544R mutant
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