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Zinc-bundle structure of the essential RNA polymerase subunit RPB10 from Methanobacterium thermoautotrophicum

TitleZinc-bundle structure of the essential RNA polymerase subunit RPB10 from Methanobacterium thermoautotrophicum
Publication TypeJournal Article
Year of Publication2000
AuthorsMackereth, CD, Arrowsmith, CH, Edwards, AM, McIntosh, LP
JournalProceedings of the National Academy of Sciences of the United States of America
Volume97
Pagination6316-6321
Date PublishedJun
Type of ArticleArticle
ISBN Number0027-8424
KeywordsABC10-BETA, ARCHAEA, COMMON SUBUNITS, DOMAIN, genomics, IN-VITRO, PROTEINS, RESOLUTION, SEQUENCE, transcription
Abstract

The RNA polymerase subunit RPB10 displays a high level of conservation across archaea and eukarya and is required for cell viability in yeast, Structure determination of this RNA polymerase subunit from Methanobacterium thermoautotrophicum reveals a topology, which we term a zinc-bundle, consisting of three cu-helices stabilized by a zinc ion. The metal ion is bound within an atypical CX2CXnCC sequence motif and serves to bridge an N-terminal loop with helix 3, This represents an example of two adjacent zinc-binding Cys residues within an alpha-helix conformation. Conserved surface features of RPB10 include discrete regions of neutral, acidic, and basic residues, the latter being located around the zinc-binding site. One or more of these regions may contribute to the role of this subunit as a scaffold protein within the polymerase holoenzyme.

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