1HMJ
SOLUTION STRUCTURE OF RNA POLYMERASE SUBUNIT H
Summary for 1HMJ
Entry DOI | 10.2210/pdb1hmj/pdb |
Descriptor | PROTEIN (SUBUNIT H) (1 entity in total) |
Functional Keywords | rna polymerase, subunit h, rpb5, archaea |
Biological source | Methanocaldococcus jannaschii |
Total number of polymer chains | 1 |
Total formula weight | 9016.68 |
Authors | Thiru, A.,Hodach, M.,Eloranta, J.,Kostourou, V.,Weinzierl, R. (deposition date: 1999-02-05, release date: 1999-04-05, Last modification date: 2023-12-27) |
Primary citation | Thiru, A.,Hodach, M.,Eloranta, J.J.,Kostourou, V.,Weinzierl, R.O.,Matthews, S. RNA polymerase subunit H features a beta-ribbon motif within a novel fold that is present in archaea and eukaryotes. J.Mol.Biol., 287:753-760, 1999 Cited by PubMed Abstract: 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. PubMed: 10191143DOI: 10.1006/jmbi.1999.2638 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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