RNA polymerase subunit H features a beta-ribbon motif within a novel fold that is present in archaea and eukaryotes.
The archaeal H and eukaryotic RPB5 RNA polymerase subunits are highly homologous and are likely to play a fundamental role in transcription that extends from archaea to humans. We report the structure of subunit H, in solution, from the archaeon Methanococcus jannaschii using multidimensional nuclear magnetic resonance. The structure reveals a novel fold containing a four-stranded mixed beta sheet that is flanked on one side by three short helices. The dominant feature is beta-ribbon motif, which presents a hydrophobic, basic surface, and defines a general RNA polymerase architectural scaffold.
Thiru
A
A
Department of Biochemistry, Imperial College of Science Technology and Medicine, Exhibition Road, London, South Kensington, SW7 2AY, UK.
Hodach
M
M
Eloranta
J J
JJ
Kostourou
V
V
Weinzierl
R O
RO
Matthews
S
S
D000595:Amino Acid Sequence; D001483:Base Sequence; D018360:Crystallography, X-Ray; D017931:DNA Primers; D012321:DNA-Directed RNA Polymerases / Q000737:chemistry*; D004795:Enzyme Stability; D005057:Eukaryotic Cells / Q000201:enzymology; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D017017:Methanococcus / Q000201:enzymology*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017510:Protein Folding; D011994:Recombinant Proteins / Q000737:chemistry; D017386:Sequence Homology, Amino Acid
D017931:DNA Primers; D011994:Recombinant Proteins; D012321:DNA-Directed RNA Polymerases