1hqm
From Proteopedia
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CRYSTAL STRUCTURE OF THERMUS AQUATICUS CORE RNA POLYMERASE-INCLUDES COMPLETE STRUCTURE WITH SIDE-CHAINS (EXCEPT FOR DISORDERED REGIONS)-FURTHER REFINED FROM ORIGINAL DEPOSITION-CONTAINS ADDITIONAL SEQUENCE INFORMATION
Overview
Bacterial DNA-dependent RNA polymerase (RNAP) has subunit composition, beta'betaalpha(I)alpha(II)omega. The role of omega has been unclear. We, show that omega is homologous in sequence and structure to RPB6, an, essential subunit shared in eukaryotic RNAP I, II, and III. In Escherichia, coli, overproduction of omega suppresses the assembly defect caused by, substitution of residue 1362 of the largest subunit of RNAP, beta'. In, yeast, overproduction of RPB6 suppresses the assembly defect caused by the, equivalent substitution in the largest subunit of RNAP II, RPB1., High-resolution structural analysis of the omega-beta' interface in, bacterial RNAP, and comparison with the RPB6-RPB1 interface in yeast RNAP, II, confirms the structural relationship and suggests a "latching", mechanism for the role of omega and RPB6 in promoting RNAP assembly.
About this Structure
1HQM is a Protein complex structure of sequences from Thermus aquaticus with MG and ZN as ligands. This structure superseeds the now removed PDB entry 1DDQ. Active as DNA-directed RNA polymerase, with EC number 2.7.7.6 Full crystallographic information is available from OCA.
Reference
Bacterial RNA polymerase subunit omega and eukaryotic RNA polymerase subunit RPB6 are sequence, structural, and functional homologs and promote RNA polymerase assembly., Minakhin L, Bhagat S, Brunning A, Campbell EA, Darst SA, Ebright RH, Severinov K, Proc Natl Acad Sci U S A. 2001 Jan 30;98(3):892-7. PMID:11158566
Page seeded by OCA on Tue Nov 20 16:45:08 2007
