6dve
From Proteopedia
Crystal structure of Mycobacterium tuberculosis transcription initiation complex(ECF selenomethionine-labelled sigma factor L) with 6 nt spacer
Structural highlights
FunctionRPOA_MYCTU 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 PubMedExtracytoplasmic (ECF) sigma factors, the largest class of alternative sigma factors, are related to primary sigma factors, but have simpler structures, comprising only two of six conserved functional modules in primary sigma factors: region 2 (sigmaR2) and region 4 (sigmaR4). Here, we report crystal structures of transcription initiation complexes containing Mycobacterium tuberculosis RNA polymerase (RNAP), M. tuberculosis ECF sigma factor sigma(L), and promoter DNA. The structures show that sigmaR2 and sigmaR4 of the ECF sigma factor occupy the same sites on RNAP as in primary sigma factors, show that the connector between sigmaR2 and sigmaR4 of the ECF sigma factor-although shorter and unrelated in sequence-follows the same path through RNAP as in primary sigma factors, and show that the ECF sigma factor uses the same strategy to bind and unwind promoter DNA as primary sigma factors. The results define protein-protein and protein-DNA interactions involved in ECF-sigma-factor-dependent transcription initiation. Structural basis of ECF-sigma-factor-dependent transcription initiation.,Lin W, Mandal S, Degen D, Cho MS, Feng Y, Das K, Ebright RH Nat Commun. 2019 Feb 12;10(1):710. doi: 10.1038/s41467-019-08443-3. PMID:30755604[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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