9f80: Difference between revisions
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==Crystal structure of Rv2242 regulator C-terminal fragment (161-414)== | |||
<StructureSection load='9f80' size='340' side='right'caption='[[9f80]], [[Resolution|resolution]] 2.03Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9f80]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9F80 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9F80 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]] 2.027Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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=9f80 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9f80 OCA], [https://pdbe.org/9f80 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9f80 RCSB], [https://www.ebi.ac.uk/pdbsum/9f80 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9f80 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Y2242_MYCTU Y2242_MYCTU] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
MabR (Rv2242), a PucR-type transcription factor, plays a crucial role in regulating mycolic acid biosynthesis in Mycobacterium tuberculosis. To understand its regulatory mechanisms, we determined the crystal structures of its N-terminal and C-terminal domains. The N-terminal domain adopts a globin-like fold, while the C-terminal domain comprises an alpha/beta GGDEF domain and an all-alpha effector domain with a helix-turn-helix DNA-binding motif. This unique domain combination is specific to Actinomycetes. Biochemical and computational studies suggest that full-length MabR forms both dimeric and tetrameric assemblies in solution. Structural analysis revealed two distinct dimerization interfaces within the N- and C-terminal domains, further supporting a tetrameric organization. These findings provide valuable insights into the domain architecture, oligomeric state, and potential regulatory mechanisms of MabR. | |||
Domain architecture of the Mycobacterium tuberculosis MabR (Rv2242), a member of the PucR transcription factor family.,Megalizzi V, Tanina A, Grosse C, Mirgaux M, Legrand P, Dias Mirandela G, Wohlkonig A, Bifani P, Wintjens R Heliyon. 2024 Nov 16;10(22):e40494. doi: 10.1016/j.heliyon.2024.e40494. , eCollection 2024 Nov 30. PMID:39641026<ref>PMID:39641026</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 9f80" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mycobacterium tuberculosis H37Rv]] | ||
[[Category: | [[Category: Bifani P]] | ||
[[Category: | [[Category: Dias Mirandela G]] | ||
[[Category: Grosse C]] | |||
[[Category: Legrand P]] | |||
[[Category: Megalizzi V]] | |||
[[Category: Mirgaux M]] | |||
[[Category: Tanina A]] | |||
[[Category: Wintjens R]] | |||
[[Category: Wohlkonig A]] | |||
