View source for 9fb1


==Crystal structure of Rv2242 regulator N-terminal fragment (1-160)==
<StructureSection load='9fb1' size='340' side='right'caption='[[9fb1]], [[Resolution|resolution]] 3.59&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9fb1]] is a 4 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=9FB1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9FB1 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]] 3.59&#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=9fb1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9fb1 OCA], [https://pdbe.org/9fb1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9fb1 RCSB], [https://www.ebi.ac.uk/pdbsum/9fb1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9fb1 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9fb1" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mycobacterium tuberculosis H37Rv]]
[[Category: Bifani P]]
[[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]]