1jih
From Proteopedia
(New page: 200px<br /><applet load="1jih" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jih, resolution 2.25Å" /> '''Yeast DNA Polymerase...) |
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| - | [[Image:1jih.gif|left|200px]]<br /><applet load="1jih" size=" | + | [[Image:1jih.gif|left|200px]]<br /><applet load="1jih" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1jih, resolution 2.25Å" /> | caption="1jih, resolution 2.25Å" /> | ||
'''Yeast DNA Polymerase ETA'''<br /> | '''Yeast DNA Polymerase ETA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | DNA polymerase eta is unique among eukaryotic polymerases in its | + | DNA polymerase eta is unique among eukaryotic polymerases in its proficient ability to replicate through a variety of distorting DNA lesions. We report here the crystal structure of the catalytic core of S. cerevisiae DNA polymerase eta, determined at 2.25A resolution. The structure reveals a novel polydactyl right hand-shaped molecule with a unique polymerase-associated domain. We identify the catalytic residues and show that the fingers and thumb domains are unusually small and stubby. In particular, the unexpected absence of helices "O" and "O1" in the fingers domain suggests that openness of the active site is the critical feature which enables DNA polymerase eta to replicate through DNA lesions such as a UV-induced cis-syn thymine-thymine dimer. |
==About this Structure== | ==About this Structure== | ||
| - | 1JIH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http:// | + | 1JIH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JIH OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Aggarwal, A | + | [[Category: Aggarwal, A K.]] |
| - | [[Category: Escalante, C | + | [[Category: Escalante, C R.]] |
| - | [[Category: Johnson, R | + | [[Category: Johnson, R E.]] |
[[Category: Prakash, L.]] | [[Category: Prakash, L.]] | ||
[[Category: Prakash, S.]] | [[Category: Prakash, S.]] | ||
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[[Category: yeast]] | [[Category: yeast]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:23:02 2008'' |
Revision as of 11:23, 21 February 2008
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Yeast DNA Polymerase ETA
Overview
DNA polymerase eta is unique among eukaryotic polymerases in its proficient ability to replicate through a variety of distorting DNA lesions. We report here the crystal structure of the catalytic core of S. cerevisiae DNA polymerase eta, determined at 2.25A resolution. The structure reveals a novel polydactyl right hand-shaped molecule with a unique polymerase-associated domain. We identify the catalytic residues and show that the fingers and thumb domains are unusually small and stubby. In particular, the unexpected absence of helices "O" and "O1" in the fingers domain suggests that openness of the active site is the critical feature which enables DNA polymerase eta to replicate through DNA lesions such as a UV-induced cis-syn thymine-thymine dimer.
About this Structure
1JIH is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Structure of the catalytic core of S. cerevisiae DNA polymerase eta: implications for translesion DNA synthesis., Trincao J, Johnson RE, Escalante CR, Prakash S, Prakash L, Aggarwal AK, Mol Cell. 2001 Aug;8(2):417-26. PMID:11545743
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