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1jaj

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|ACTIVITY=
|ACTIVITY=
|GENE= O174L ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10497 African swine fever virus])
|GENE= O174L ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10497 African swine fever virus])
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|DOMAIN=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jaj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jaj OCA], [http://www.ebi.ac.uk/pdbsum/1jaj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jaj RCSB]</span>
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[[Category: cis peptide]]
[[Category: cis peptide]]
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Revision as of 18:30, 30 March 2008


PDB ID 1jaj

Drag the structure with the mouse to rotate
Gene: O174L (African swine fever virus)
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Solution Structure of DNA Polymerase X from the African Swine Fever Virus


Overview

DNA polymerase X (Pol X) from the African swine fever virus (ASFV) specifically binds intermediates in the single-nucleotide base-excision repair process, an activity indicative of repair function. In addition, Pol X catalyzes DNA polymerization with low nucleotide-insertion fidelity. The structural mechanisms by which DNA polymerases confer high or low fidelity in DNA polymerization remain to be elucidated. The three-dimensional structure of Pol X has been determined. Unlike other DNA polymerases, Pol X is formed from only a palm and a C-terminal subdomain. Pol X has a novel palm subdomain fold, containing a positively charged helix at the DNA binding surface. Purine deoxynucleoside triphosphate (dNTP) substrates bind between the palm and C-terminal subdomain, at a dNTP-binding helix, and induce a unique conformation in Pol X. The purine dNTP-bound conformation and high binding affinity for dGTP-Mg(2+) of Pol X may contribute to its low fidelity.

About this Structure

1JAJ is a Single protein structure of sequence from African swine fever virus. Full crystallographic information is available from OCA.

Reference

Solution structure of a viral DNA repair polymerase., Maciejewski MW, Shin R, Pan B, Marintchev A, Denninger A, Mullen MA, Chen K, Gryk MR, Mullen GP, Nat Struct Biol. 2001 Nov;8(11):936-41. PMID:11685238

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