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Publication Abstract from PubMed
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 alpha-helices stabilized by a zinc ion. The metal ion is bound within an atypical CX(2)CX(n)CC 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.
Zinc-bundle structure of the essential RNA polymerase subunit RPB10 from Methanobacterium thermoautotrophicum.,Mackereth CD, Arrowsmith CH, Edwards AM, McIntosh LP Proc Natl Acad Sci U S A. 2000 Jun 6;97(12):6316-21. PMID:10841539[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑Mackereth CD, Arrowsmith CH, Edwards AM, McIntosh LP. Zinc-bundle structure of the essential RNA polymerase subunit RPB10 from Methanobacterium thermoautotrophicum. Proc Natl Acad Sci U S A. 2000 Jun 6;97(12):6316-21. PMID:10841539
