1dd9
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(New page: 200px<br /><applet load="1dd9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dd9, resolution 1.6Å" /> '''STRUCTURE OF THE DNAG...)
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Revision as of 11:04, 20 November 2007
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STRUCTURE OF THE DNAG CATALYTIC CORE
Overview
All cellular organisms use specialized RNA polymerases called "primases", to synthesize RNA primers for the initiation of DNA replication. The, high-resolution crystal structure of a primase, comprising the catalytic, core of the Escherichia coli DnaG protein, was determined. The core, structure contains an active-site architecture that is unrelated to other, DNA or RNA polymerase palm folds, but is instead related to the "toprim", fold. On the basis of the structure, it is likely that DnaG binds nucleic, acid in a groove clustered with invariant residues and that DnaG is, positioned within the replisome to accept single-stranded DNA directly, from the replicative helicase.
About this Structure
1DD9 is a Single protein structure of sequence from Escherichia coli with SR as ligand. Full crystallographic information is available from OCA.
Reference
Structure of the RNA polymerase domain of E. coli primase., Keck JL, Roche DD, Lynch AS, Berger JM, Science. 2000 Mar 31;287(5462):2482-6. PMID:10741967
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