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FEBS Lett ; 593(9): 996-1005, 2019 05.
Artículo en Inglés | MEDLINE | ID: mdl-30972737

RESUMEN

The HelD is a helicase-like protein binding to Bacillus subtilis RNA polymerase (RNAP), stimulating transcription in an ATP-dependent manner. Here, our small angle X-ray scattering data bring the first insights into the HelD structure: HelD is compact in shape and undergoes a conformational change upon substrate analog binding. Furthermore, the HelD domain structure is delineated, and a partial model of HelD is presented. In addition, the unique N-terminal domain of HelD is characterized as essential for its transcription-related function but not for ATPase activity, DNA binding, or binding to RNAP. The study provides a topological basis for further studies of the role of HelD in transcription.


Asunto(s)
Bacillus subtilis/enzimología , Proteínas Bacterianas/química , Proteínas Bacterianas/metabolismo , ARN Polimerasas Dirigidas por ADN/metabolismo , Modelos Moleculares , Unión Proteica , Dominios Proteicos , Dispersión del Ángulo Pequeño , Difracción de Rayos X
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