7oqh: Difference between revisions

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<StructureSection load='7oqh' size='340' side='right'caption='[[7oqh]], [[Resolution|resolution]] 3.32&Aring;' scene=''>
<StructureSection load='7oqh' size='340' side='right'caption='[[7oqh]], [[Resolution|resolution]] 3.32&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7oqh]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OQH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OQH FirstGlance]. <br>
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OQH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OQH FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.32&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <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=7oqh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7oqh OCA], [https://pdbe.org/7oqh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7oqh RCSB], [https://www.ebi.ac.uk/pdbsum/7oqh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7oqh 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=7oqh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7oqh OCA], [https://pdbe.org/7oqh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7oqh RCSB], [https://www.ebi.ac.uk/pdbsum/7oqh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7oqh ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/RHO_MYCTU RHO_MYCTU]] Facilitates transcription termination by a mechanism that involves Rho binding to the nascent RNA, activation of Rho's RNA-dependent ATPase activity, and release of the mRNA from the DNA template. Shows poor RNA-dependent ATP hydrolysis and inefficient DNA-RNA unwinding activities, but exhibits robust and fast transcription termination, which suggests that the transcription termination function of M.tuberculosis Rho is not correlated with its helicase/translocase activities and that these functions may not be important for its RNA release process.[HAMAP-Rule:MF_01884]<ref>PMID:20026069</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The bacterial Rho factor is a ring-shaped motor triggering genome-wide transcription termination and R-loop dissociation. Rho is essential in many species, including in Mycobacterium tuberculosis where rho gene inactivation leads to rapid death. Yet, the M. tuberculosis Rho [MtbRho] factor displays poor NTPase and helicase activities, and resistance to the natural Rho inhibitor bicyclomycin [BCM] that remain unexplained. To address these issues, we solved the cryo-EM structure of MtbRho at 3.3 A resolution. The MtbRho hexamer is poised into a pre-catalytic, open-ring state wherein specific contacts stabilize ATP in intersubunit ATPase pockets, thereby explaining the cofactor preference of MtbRho. We reveal a leucine-to-methionine substitution that creates a steric bulk in BCM binding cavities near the positions of ATP gamma-phosphates, and confers resistance to BCM at the expense of motor efficiency. Our work contributes to explain the unusual features of MtbRho and provides a framework for future antibiotic development.


Cryo-EM structure of transcription termination factor Rho from Mycobacterium tuberculosis reveals bicyclomycin resistance mechanism.,Saridakis E, Vishwakarma R, Lai-Kee-Him J, Martin K, Simon I, Cohen-Gonsaud M, Coste F, Bron P, Margeat E, Boudvillain M Commun Biol. 2022 Feb 9;5(1):120. doi: 10.1038/s42003-022-03069-6. PMID:35140348<ref>PMID:35140348</ref>
==See Also==
 
*[[Helicase 3D structures|Helicase 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7oqh" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Boudvillain M]]
[[Category: Boudvillain M]]
[[Category: Bron P]]
[[Category: Bron P]]

Latest revision as of 12:28, 17 July 2024

CryoEM structure of the transcription termination factor Rho from Mycobacterium tuberculosis

7oqh, resolution 3.32Å

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