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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'''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==
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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.
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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==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JAJ OCA].
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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]]
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[[Category: Maciejewski, M.W.]]
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[[Category: Maciejewski, M W.]]
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[[Category: Mullen, G.P.]]
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[[Category: Mullen, G P.]]
[[Category: Pan, B.]]
[[Category: Pan, B.]]
[[Category: Shin, R.]]
[[Category: Shin, R.]]
[[Category: cis peptide]]
[[Category: cis peptide]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:03:14 2007''
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''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


1jaj

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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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