1dde: Difference between revisions
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dde FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dde OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dde RCSB], [http://www.ebi.ac.uk/pdbsum/1dde PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dde FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dde OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dde RCSB], [http://www.ebi.ac.uk/pdbsum/1dde PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/PRIM_ECOLI PRIM_ECOLI]] DNA primase is the polymerase that synthesizes small RNA primers for the Okazaki fragments on both template strands at replication forks during chromosomal DNA synthesis. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 18:23, 25 December 2014
STRUCTURE OF THE DNAG CATALYTIC CORESTRUCTURE OF THE DNAG CATALYTIC CORE
Structural highlights
Function[PRIM_ECOLI] DNA primase is the polymerase that synthesizes small RNA primers for the Okazaki fragments on both template strands at replication forks during chromosomal DNA synthesis. 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 PubMedAll 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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