1jaj
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(New page: 200px<br /><applet load="1jaj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jaj" /> '''Solution Structure of DNA Polymerase X from ...)
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Revision as of 15:56, 20 November 2007
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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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