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SOLUTION STRUCTURE OF THE ESSENTIAL RNA POLYMERASE SUBUNIT RPB10 FROM METHANOBACTERIUM THERMOAUTOTROPHICUM

Overview

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.

About this Structure

1EF4 is a Single protein structure of sequence from Methanothermobacter thermautotrophicus with ZN as ligand. Active as DNA-directed RNA polymerase, with EC number 2.7.7.6 Full crystallographic information is available from OCA.

Reference

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

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