1xi1

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[[Image:1xi1.gif|left|200px]]
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{{Seed}}
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[[Image:1xi1.png|left|200px]]
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{{STRUCTURE_1xi1| PDB=1xi1 | SCENE= }}
{{STRUCTURE_1xi1| PDB=1xi1 | SCENE= }}
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'''Phi29 DNA polymerase ssDNA complex, monoclinic crystal form'''
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===Phi29 DNA polymerase ssDNA complex, monoclinic crystal form===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15546620 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15546620}}
==About this Structure==
==About this Structure==
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[[Category: Replication]]
[[Category: Replication]]
[[Category: Strand displacement]]
[[Category: Strand displacement]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:23:47 2008''

Revision as of 03:23, 28 July 2008

Image:1xi1.png

Template:STRUCTURE 1xi1

Phi29 DNA polymerase ssDNA complex, monoclinic crystal form

Template:ABSTRACT PUBMED 15546620

About this Structure

1XI1 is a Single protein structure of sequence from Bacillus phage phi29. 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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