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| [[Image:2pyl.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_2pyl| PDB=2pyl | SCENE= }} | | {{STRUCTURE_2pyl| PDB=2pyl | SCENE= }} |
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| '''Phi29 DNA polymerase complexed with primer-template DNA and incoming nucleotide substrates (ternary complex)'''
| | ===Phi29 DNA polymerase complexed with primer-template DNA and incoming nucleotide substrates (ternary complex)=== |
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| ==Overview==
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| Replicative DNA polymerases (DNAPs) move along template DNA in a processive manner. The structural basis of the mechanism of translocation has been better studied in the A-family of polymerases than in the B-family of replicative polymerases. To address this issue, we have determined the X-ray crystal structures of phi29 DNAP, a member of the protein-primed subgroup of the B-family of polymerases, complexed with primer-template DNA in the presence or absence of the incoming nucleoside triphosphate, the pre- and post-translocated states, respectively. Comparison of these structures reveals a mechanism of translocation that appears to be facilitated by the coordinated movement of two conserved tyrosine residues into the insertion site. This differs from the mechanism employed by the A-family polymerases, in which a conserved tyrosine moves into the templating and insertion sites during the translocation step. Polymerases from the two families also interact with downstream single-stranded template DNA in very different ways.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17611604}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17611604 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17611604}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Vega, M de.]] | | [[Category: Vega, M de.]] |
| [[Category: Protein-dna complex]] | | [[Category: Protein-dna complex]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 14:01:17 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 16:08:09 2008'' |
