6znr: Difference between revisions
New page: '''Unreleased structure''' The entry 6znr is ON HOLD Authors: Lovering, A.L., Harding, C.J. Description: MaeB PTA domain R535A mutant Category: Unreleased Structures [[Category: Ha... |
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==MaeB PTA domain R535A mutant== | |||
<StructureSection load='6znr' size='340' side='right'caption='[[6znr]], [[Resolution|resolution]] 2.22Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6znr]] 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=6ZNR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZNR 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]] 2.217Å</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=6znr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6znr OCA], [https://pdbe.org/6znr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6znr RCSB], [https://www.ebi.ac.uk/pdbsum/6znr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6znr 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 6znr" 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]] | |||
Latest revision as of 14:55, 1 February 2024
MaeB PTA domain R535A mutantMaeB PTA domain R535A mutant
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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