1ef4
From Proteopedia
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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 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
Page seeded by OCA on Thu Feb 21 12:27:03 2008
Categories: DNA-directed RNA polymerase | Methanothermobacter thermautotrophicus | Single protein | Arrowsmith, C H. | Edwards, A M. | Mackereth, C D. | Mcintosh, L P. | NESG, Northeast Structural Genomics Consortium. | ZN | Nesg | Northeast structural genomics consortium | Protein structure initiative | Psi | Structural genomics | Three helix bundle | Zinc binding
