5vi5: Difference between revisions
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==Structure of Mycobacterium smegmatis transcription initiation complex with a full transcription bubble== | |||
<StructureSection load='5vi5' size='340' side='right'caption='[[5vi5]], [[Resolution|resolution]] 3.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5vi5]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_smegmatis_MC2_155 Mycolicibacterium smegmatis MC2 155] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VI5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VI5 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]] 3.196Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=5vi5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vi5 OCA], [https://pdbe.org/5vi5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vi5 RCSB], [https://www.ebi.ac.uk/pdbsum/5vi5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vi5 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/RPOA_MYCS2 RPOA_MYCS2] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[HAMAP-Rule:MF_00059]<ref>PMID:19926651</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The mycobacteria RNA polymerase (RNAP) is a target for antimicrobials against tuberculosis, motivating structure/function studies. Here we report a 3.2 A-resolution crystal structure of a Mycobacterium smegmatis (Msm) open promoter complex (RPo), along with structural analysis of the Msm RPo and a previously reported 2.76 A-resolution crystal structure of an Msm transcription initiation complex with a promoter DNA fragment. We observe the interaction of the Msm RNAP alpha-subunit C-terminal domain (alphaCTD) with DNA, and we provide evidence that the alphaCTD may play a role in Mtb transcription regulation. Our results reveal the structure of an Actinobacteria-unique insert of the RNAP beta' subunit. Finally, our analysis reveals the disposition of the N-terminal segment of Msm sigmaA, which may comprise an intrinsically disordered protein domain unique to mycobacteria. The clade-specific features of the mycobacteria RNAP provide clues to the profound instability of mycobacteria RPo compared with E. coli. | |||
Structural insights into the mycobacteria transcription initiation complex from analysis of X-ray crystal structures.,Hubin EA, Lilic M, Darst SA, Campbell EA Nat Commun. 2017 Jul 13;8:16072. doi: 10.1038/ncomms16072. PMID:28703128<ref>PMID:28703128</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5vi5" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Sigma factor 3D structures|Sigma factor 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mycolicibacterium smegmatis MC2 155]] | |||
[[Category: Synthetic construct]] | |||
[[Category: Campbell EA]] | |||
[[Category: Darst SA]] | |||
[[Category: Lilic M]] | |||
Latest revision as of 16:49, 4 October 2023
Structure of Mycobacterium smegmatis transcription initiation complex with a full transcription bubbleStructure of Mycobacterium smegmatis transcription initiation complex with a full transcription bubble
Structural highlights
FunctionRPOA_MYCS2 DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[HAMAP-Rule:MF_00059][1] Publication Abstract from PubMedThe mycobacteria RNA polymerase (RNAP) is a target for antimicrobials against tuberculosis, motivating structure/function studies. Here we report a 3.2 A-resolution crystal structure of a Mycobacterium smegmatis (Msm) open promoter complex (RPo), along with structural analysis of the Msm RPo and a previously reported 2.76 A-resolution crystal structure of an Msm transcription initiation complex with a promoter DNA fragment. We observe the interaction of the Msm RNAP alpha-subunit C-terminal domain (alphaCTD) with DNA, and we provide evidence that the alphaCTD may play a role in Mtb transcription regulation. Our results reveal the structure of an Actinobacteria-unique insert of the RNAP beta' subunit. Finally, our analysis reveals the disposition of the N-terminal segment of Msm sigmaA, which may comprise an intrinsically disordered protein domain unique to mycobacteria. The clade-specific features of the mycobacteria RNAP provide clues to the profound instability of mycobacteria RPo compared with E. coli. Structural insights into the mycobacteria transcription initiation complex from analysis of X-ray crystal structures.,Hubin EA, Lilic M, Darst SA, Campbell EA Nat Commun. 2017 Jul 13;8:16072. doi: 10.1038/ncomms16072. PMID:28703128[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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