|Proceedings of the National Academy of Sciences of the United States of America (2000) 97(12):6316-21|
|Northeast Structural Genomics Consortium|
(click to unfold)
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.
|metabolism chemistry enzymology |
|Binding Sites Amino Acid Sequence Molecular Sequence Data Protein Structure, Secondary Protein Folding Methanobacterium Zinc RNA DNA DNA-Directed RNA Polymerases |
|16 (Last update: 03/16/2019 1:54:33pm)|
|Proc Natl Acad Sci U S A. 2000 Jun 6;97(12):6316-21.|