6znr: Difference between revisions

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-'''Unreleased structure'''
-The entry 6znr is ON HOLD  until Paper Publication
+==MaeB PTA domain R535A mutant==
+<StructureSection load='6znr' size='340' side='right'caption='[[6znr]], [[Resolution|resolution]] 2.22&Aring;' 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]] 2.217&#8491;</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.
-Authors: Lovering, A.L., Harding, C.J.
+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>
-Description: MaeB PTA domain R535A mutant
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Harding, C.J]]
+<div class="pdbe-citations 6znr" style="background-color:#fffaf0;"></div>
-[[Category: Lovering, A.L]]
+==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]]