6zn4: Difference between revisions
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<StructureSection load='6zn4' size='340' side='right'caption='[[6zn4]], [[Resolution|resolution]] 1.68Å' scene=''> | <StructureSection load='6zn4' size='340' side='right'caption='[[6zn4]], [[Resolution|resolution]] 1.68Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6zn4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[6zn4]] is a 2 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=6ZN4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZN4 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.679Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=6zn4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zn4 OCA], [https://pdbe.org/6zn4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zn4 RCSB], [https://www.ebi.ac.uk/pdbsum/6zn4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zn4 ProSAT]</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=6zn4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zn4 OCA], [https://pdbe.org/6zn4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zn4 RCSB], [https://www.ebi.ac.uk/pdbsum/6zn4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zn4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q6MM15_BDEBA Q6MM15_BDEBA] [https://www.uniprot.org/uniprot/Q6MM14_BDEBA Q6MM14_BDEBA] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 6zn4" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6zn4" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Malate Dehydrogenase 3D structures|Malate Dehydrogenase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bdellovibrio bacteriovorus HD100]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Harding | [[Category: Harding CJ]] | ||
[[Category: Lovering | [[Category: Lovering AL]] | ||
Latest revision as of 14:54, 1 February 2024
MaeB malic enzyme domain apoproteinMaeB malic enzyme domain apoprotein
Structural highlights
FunctionPublication Abstract from PubMedBacterial 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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