2ex3
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:2ex3.gif|left|200px]] | + | [[Image:2ex3.gif|left|200px]] |
| - | + | ||
| - | '''Bacteriophage phi29 DNA polymerase bound to terminal protein''' | + | {{Structure |
| + | |PDB= 2ex3 |SIZE=350|CAPTION= <scene name='initialview01'>2ex3</scene>, resolution 3.000Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=PB:LEAD (II) ION'>PB</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] | ||
| + | |GENE= 2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=221993 Vibrio phage f237]), 3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=221993 Vibrio phage f237]) | ||
| + | }} | ||
| + | |||
| + | '''Bacteriophage phi29 DNA polymerase bound to terminal protein''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2EX3 is a [ | + | 2EX3 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Vibrio_phage_f237 Vibrio phage f237]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EX3 OCA]. |
==Reference== | ==Reference== | ||
| - | The phi29 DNA polymerase:protein-primer structure suggests a model for the initiation to elongation transition., Kamtekar S, Berman AJ, Wang J, Lazaro JM, de Vega M, Blanco L, Salas M, Steitz TA, EMBO J. 2006 Mar 22;25(6):1335-43. Epub 2006 Mar 2. PMID:[http:// | + | The phi29 DNA polymerase:protein-primer structure suggests a model for the initiation to elongation transition., Kamtekar S, Berman AJ, Wang J, Lazaro JM, de Vega M, Blanco L, Salas M, Steitz TA, EMBO J. 2006 Mar 22;25(6):1335-43. Epub 2006 Mar 2. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16511564 16511564] |
[[Category: DNA-directed DNA polymerase]] | [[Category: DNA-directed DNA polymerase]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| Line 24: | Line 33: | ||
[[Category: dna polymerase: protein primer complex]] | [[Category: dna polymerase: protein primer complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:45:26 2008'' |
Revision as of 14:45, 20 March 2008
| |||||||
| , resolution 3.000Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | 2 (Vibrio phage f237), 3 (Vibrio phage f237) | ||||||
| Activity: | DNA-directed DNA polymerase, with EC number 2.7.7.7 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Bacteriophage phi29 DNA polymerase bound to terminal protein
Overview
The absolute requirement for primers in the initiation of DNA synthesis poses a problem for replicating the ends of linear chromosomes. The DNA polymerase of bacteriophage phi29 solves this problem by using a serine hydroxyl of terminal protein to prime replication. The 3.0 A resolution structure shows one domain of terminal protein making no interactions, a second binding the polymerase and a third domain containing the priming serine occupying the same binding cleft in the polymerase as duplex DNA does during elongation. Thus, the progressively elongating DNA duplex product must displace this priming domain. Further, this heterodimer of polymerase and terminal protein cannot accommodate upstream template DNA, thereby explaining its specificity for initiating DNA synthesis only at the ends of the bacteriophage genome. We propose a model for the transition from the initiation to the elongation phases in which the priming domain of terminal protein moves out of the active site as polymerase elongates the primer strand. The model indicates that terminal protein should dissociate from polymerase after the incorporation of approximately six nucleotides.
About this Structure
2EX3 is a Protein complex structure of sequences from Vibrio phage f237. Full crystallographic information is available from OCA.
Reference
The phi29 DNA polymerase:protein-primer structure suggests a model for the initiation to elongation transition., Kamtekar S, Berman AJ, Wang J, Lazaro JM, de Vega M, Blanco L, Salas M, Steitz TA, EMBO J. 2006 Mar 22;25(6):1335-43. Epub 2006 Mar 2. PMID:16511564
Page seeded by OCA on Thu Mar 20 16:45:26 2008
