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1dd9

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{{STRUCTURE_1dd9| PDB=1dd9 | SCENE= }}
{{STRUCTURE_1dd9| PDB=1dd9 | SCENE= }}
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'''STRUCTURE OF THE DNAG CATALYTIC CORE'''
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===STRUCTURE OF THE DNAG CATALYTIC CORE===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_10741967}}
==About this Structure==
==About this Structure==
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[[Category: Rna polymerase]]
[[Category: Rna polymerase]]
[[Category: Toprim]]
[[Category: Toprim]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:43:09 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 22:51:15 2008''

Revision as of 19:51, 30 June 2008

Image:1dd9.png

Template:STRUCTURE 1dd9

STRUCTURE OF THE DNAG CATALYTIC CORE

Template:ABSTRACT PUBMED 10741967

About this Structure

1DD9 is a Single protein structure of sequence from Escherichia coli. 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

Page seeded by OCA on Mon Jun 30 22:51:15 2008

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