1s5j
From Proteopedia
(New page: 200px<br /><applet load="1s5j" size="450" color="white" frame="true" align="right" spinBox="true" caption="1s5j, resolution 2.40Å" /> '''Insight in DNA Repli...) |
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| - | [[Image:1s5j.jpg|left|200px]]<br /><applet load="1s5j" size=" | + | [[Image:1s5j.jpg|left|200px]]<br /><applet load="1s5j" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1s5j, resolution 2.40Å" /> | caption="1s5j, resolution 2.40Å" /> | ||
'''Insight in DNA Replication: The crystal structure of DNA Polymerase B1 from the archaeon Sulfolobus solfataricus'''<br /> | '''Insight in DNA Replication: The crystal structure of DNA Polymerase B1 from the archaeon Sulfolobus solfataricus'''<br /> | ||
==Overview== | ==Overview== | ||
| - | To minimize the large number of mispairs during genome duplication owing | + | To minimize the large number of mispairs during genome duplication owing to the large amount of DNA to be synthesized, many replicative polymerases have accessory domains with complementary functions. We describe the crystal structure of replicative DNA polymerase B1 from the archaeon Sulfolobus solfataricus. Comparison between other known structures indicates that although the protein is folded into the typical N-terminal, editing 3'-5'exonuclease, and C-terminal right-handed polymerase domains, it is characterized by the unusual presence of two extra alpha helices in the N-terminal domain interacting with the fingers helices to form an extended fingers subdomain, a structural feature that can account for some functional features of the protein. We explore the structural basis of specific lesion recognition, the initial step in DNA repair, describing how the N-terminal subdomain pocket of archaeal DNA polymerases could allow specific recognition of deaminated bases such as uracil and hypoxanthine in addition to the typical DNA bases. |
==About this Structure== | ==About this Structure== | ||
| - | 1S5J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus] with SO4 and MG as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] Full crystallographic information is available from [http:// | + | 1S5J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S5J OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Sulfolobus solfataricus]] | [[Category: Sulfolobus solfataricus]] | ||
[[Category: Federici, L.]] | [[Category: Federici, L.]] | ||
| - | [[Category: Johnson, K | + | [[Category: Johnson, K A.]] |
[[Category: Nastopoulos, V.]] | [[Category: Nastopoulos, V.]] | ||
| - | [[Category: Pisani, F | + | [[Category: Pisani, F M.]] |
[[Category: Rossi, M.]] | [[Category: Rossi, M.]] | ||
[[Category: Savino, C.]] | [[Category: Savino, C.]] | ||
| Line 27: | Line 27: | ||
[[Category: replication]] | [[Category: replication]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:58:18 2008'' |
Revision as of 12:58, 21 February 2008
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Insight in DNA Replication: The crystal structure of DNA Polymerase B1 from the archaeon Sulfolobus solfataricus
Overview
To minimize the large number of mispairs during genome duplication owing to the large amount of DNA to be synthesized, many replicative polymerases have accessory domains with complementary functions. We describe the crystal structure of replicative DNA polymerase B1 from the archaeon Sulfolobus solfataricus. Comparison between other known structures indicates that although the protein is folded into the typical N-terminal, editing 3'-5'exonuclease, and C-terminal right-handed polymerase domains, it is characterized by the unusual presence of two extra alpha helices in the N-terminal domain interacting with the fingers helices to form an extended fingers subdomain, a structural feature that can account for some functional features of the protein. We explore the structural basis of specific lesion recognition, the initial step in DNA repair, describing how the N-terminal subdomain pocket of archaeal DNA polymerases could allow specific recognition of deaminated bases such as uracil and hypoxanthine in addition to the typical DNA bases.
About this Structure
1S5J is a Single protein structure of sequence from Sulfolobus solfataricus with and as ligands. Active as DNA-directed DNA polymerase, with EC number 2.7.7.7 Full crystallographic information is available from OCA.
Reference
Insights into DNA replication: the crystal structure of DNA polymerase B1 from the archaeon Sulfolobus solfataricus., Savino C, Federici L, Johnson KA, Vallone B, Nastopoulos V, Rossi M, Pisani FM, Tsernoglou D, Structure. 2004 Nov;12(11):2001-8. PMID:15530364
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