1eik | pdb_00001eik

Solution Structure of RNA Polymerase Subunit RPB5 from Methanobacterium Thermoautotrophicum

spinqualitylabelsall models 1eik, 10 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1eik is a 1 chain structure with sequence from "methanobacterium_thermoautotrophicus"_(sic)_zeikus_and_wolfe_1972 "methanobacterium thermoautotrophicus" (sic) zeikus and wolfe 1972. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Activity: DNA-directed RNA polymerase, with EC number 2.7.7.6 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN Function [RPOH_METTH] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed RPB5 is an essential subunit of eukaryotic and archaeal RNA polymerases. It is a proposed target for transcription activator proteins in eukaryotes, but the mechanism of interaction is not known. We have determined the solution structure of the RPB5 subunit from the thermophilic archeon, Methanobacterium thermoautotrophicum. MtRBP5 contains a four-stranded beta-sheet platform supporting two alpha-helices, one on each side of the beta-sheet, resulting in an overall mushroom shape that does not appear to have any structural homologues in the structural database. The position and conservation of charged surface residues suggests possible modes of interaction with other proteins, as well as a rationale for the thermal stability of this protein. Solution structure of the RNA polymerase subunit RPB5 from Methanobacterium thermoautotrophicum.,Yee A, Booth V, Dharamsi A, Engel A, Edwards AM, Arrowsmith CH Proc Natl Acad Sci U S A. 2000 Jun 6;97(12):6311-5. PMID:10841538 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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