2py5
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Replicative DNA polymerases (DNAPs) move along template DNA in a | + | 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. |
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | Structures of phi29 DNA polymerase complexed with substrate: the mechanism of translocation in B-family polymerases., Berman AJ, Kamtekar S, Goodman JL, Lazaro JM, de Vega M, Blanco L, Salas M, Steitz TA, EMBO J. 2007 Jul | + | Structures of phi29 DNA polymerase complexed with substrate: the mechanism of translocation in B-family polymerases., Berman AJ, Kamtekar S, Goodman JL, Lazaro JM, de Vega M, Blanco L, Salas M, Steitz TA, EMBO J. 2007 Jul 25;26(14):3494-505. Epub 2007 Jul 5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17611604 17611604] |
[[Category: DNA-directed DNA polymerase]] | [[Category: DNA-directed DNA polymerase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Vibrio phage f237]] | [[Category: Vibrio phage f237]] | ||
| - | [[Category: Berman, A | + | [[Category: Berman, A J.]] |
[[Category: Blanco, L.]] | [[Category: Blanco, L.]] | ||
| - | [[Category: Goodman, J | + | [[Category: Goodman, J L.]] |
[[Category: Kamtekar, S.]] | [[Category: Kamtekar, S.]] | ||
| - | [[Category: Lazaro, J | + | [[Category: Lazaro, J M.]] |
[[Category: Salas, M.]] | [[Category: Salas, M.]] | ||
| - | [[Category: Steitz, T | + | [[Category: Steitz, T A.]] |
| - | [[Category: Vega, M | + | [[Category: Vega, M de.]] |
[[Category: EDO]] | [[Category: EDO]] | ||
[[Category: protein-dna complex]] | [[Category: protein-dna complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:34:11 2008'' |
Revision as of 16:34, 21 February 2008
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Phi29 DNA polymerase complexed with single-stranded DNA
Overview
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.
About this Structure
2PY5 is a Single protein structure of sequence from Vibrio phage f237 with as ligand. Active as DNA-directed DNA polymerase, with EC number 2.7.7.7 Full crystallographic information is available from OCA.
Reference
Structures of phi29 DNA polymerase complexed with substrate: the mechanism of translocation in B-family polymerases., Berman AJ, Kamtekar S, Goodman JL, Lazaro JM, de Vega M, Blanco L, Salas M, Steitz TA, EMBO J. 2007 Jul 25;26(14):3494-505. Epub 2007 Jul 5. PMID:17611604
Page seeded by OCA on Thu Feb 21 18:34:11 2008
