1xi1
From Proteopedia
(New page: 200px<br /><applet load="1xi1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xi1, resolution 2.20Å" /> '''Phi29 DNA polymerase...) |
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| - | [[Image:1xi1.gif|left|200px]]<br /><applet load="1xi1" size=" | + | [[Image:1xi1.gif|left|200px]]<br /><applet load="1xi1" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1xi1, resolution 2.20Å" /> | caption="1xi1, resolution 2.20Å" /> | ||
'''Phi29 DNA polymerase ssDNA complex, monoclinic crystal form'''<br /> | '''Phi29 DNA polymerase ssDNA complex, monoclinic crystal form'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The DNA polymerase from phage phi29 is a B family polymerase that | + | The DNA polymerase from phage phi29 is a B family polymerase that initiates replication using a protein as a primer, attaching the first nucleotide of the phage genome to the hydroxyl of a specific serine of the priming protein. The crystal structure of phi29 DNA polymerase determined at 2.2 A resolution provides explanations for its extraordinary processivity and strand displacement activities. Homology modeling suggests that downstream template DNA passes through a tunnel prior to entering the polymerase active site. This tunnel is too small to accommodate double-stranded DNA and requires the separation of template and nontemplate strands. Members of the B family of DNA polymerases that use protein primers contain two sequence insertions: one forms a domain not previously observed in polymerases, while the second resembles the specificity loop of T7 RNA polymerase. The high processivity of phi29 DNA polymerase may be explained by its topological encirclement of both the downstream template and the upstream duplex DNA. |
==About this Structure== | ==About this Structure== | ||
| - | 1XI1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_phage_f237 Vibrio phage f237] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | + | 1XI1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_phage_f237 Vibrio phage f237] with <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XI1 OCA]. |
==Reference== | ==Reference== | ||
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[[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: 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: Wang, J.]] | [[Category: Wang, J.]] | ||
[[Category: MG]] | [[Category: MG]] | ||
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[[Category: strand displacement]] | [[Category: strand displacement]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:55:00 2008'' |
Revision as of 13:55, 21 February 2008
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Phi29 DNA polymerase ssDNA complex, monoclinic crystal form
Overview
The DNA polymerase from phage phi29 is a B family polymerase that initiates replication using a protein as a primer, attaching the first nucleotide of the phage genome to the hydroxyl of a specific serine of the priming protein. The crystal structure of phi29 DNA polymerase determined at 2.2 A resolution provides explanations for its extraordinary processivity and strand displacement activities. Homology modeling suggests that downstream template DNA passes through a tunnel prior to entering the polymerase active site. This tunnel is too small to accommodate double-stranded DNA and requires the separation of template and nontemplate strands. Members of the B family of DNA polymerases that use protein primers contain two sequence insertions: one forms a domain not previously observed in polymerases, while the second resembles the specificity loop of T7 RNA polymerase. The high processivity of phi29 DNA polymerase may be explained by its topological encirclement of both the downstream template and the upstream duplex DNA.
About this Structure
1XI1 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
Insights into strand displacement and processivity from the crystal structure of the protein-primed DNA polymerase of bacteriophage phi29., Kamtekar S, Berman AJ, Wang J, Lazaro JM, de Vega M, Blanco L, Salas M, Steitz TA, Mol Cell. 2004 Nov 19;16(4):609-18. PMID:15546620
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