1jaj
From Proteopedia
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'''Solution Structure of DNA Polymerase X from the African Swine Fever Virus'''<br /> | '''Solution Structure of DNA Polymerase X from the African Swine Fever Virus'''<br /> | ||
==Overview== | ==Overview== | ||
- | DNA polymerase X (Pol X) from the African swine fever virus (ASFV) | + | 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== | ==About this Structure== | ||
- | 1JAJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/African_swine_fever_virus African swine fever virus]. Full crystallographic information is available from [http:// | + | 1JAJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/African_swine_fever_virus African swine fever virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JAJ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: African swine fever virus]] | [[Category: African swine fever virus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
- | [[Category: Maciejewski, M | + | [[Category: Maciejewski, M W.]] |
- | [[Category: Mullen, G | + | [[Category: Mullen, G P.]] |
[[Category: Pan, B.]] | [[Category: Pan, B.]] | ||
[[Category: Shin, R.]] | [[Category: Shin, R.]] | ||
[[Category: cis peptide]] | [[Category: cis peptide]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:20:31 2008'' |
Revision as of 11:20, 21 February 2008
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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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