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2aq4

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[[Image:2aq4.gif|left|200px]]
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{{Seed}}
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[[Image:2aq4.png|left|200px]]
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{{STRUCTURE_2aq4| PDB=2aq4 | SCENE= }}
{{STRUCTURE_2aq4| PDB=2aq4 | SCENE= }}
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'''Ternary complex of the catalytic core of REV1 with DNA and dCTP.'''
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===Ternary complex of the catalytic core of REV1 with DNA and dCTP.===
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==Overview==
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The Rev1 DNA polymerase is highly specialized for the incorporation of C opposite template G. We present here the crystal structure of yeast Rev1 bound to template G and incoming 2'-deoxycytidine 5'-triphosphate (dCTP), which reveals that the polymerase itself dictates the identity of the incoming nucleotide, as well as the identity of the templating base. Template G and incoming dCTP do not pair with each other. Instead, the template G is evicted from the DNA helix, and it makes optimal hydrogen bonds with a segment of Rev1. Also, unlike other DNA polymerases, incoming dCTP pairs with an arginine rather than the templating base, which ensures the incorporation of dCTP over other incoming nucleotides. This mechanism provides an elegant means for promoting proficient and error-free synthesis through N2-adducted guanines that obstruct replication.
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The line below this paragraph, {{ABSTRACT_PUBMED_16195463}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 16195463 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16195463}}
==About this Structure==
==About this Structure==
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[[Category: Polymerase]]
[[Category: Polymerase]]
[[Category: Rev1]]
[[Category: Rev1]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:20:02 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:57:11 2008''

Revision as of 17:57, 27 July 2008

Image:2aq4.png

Template:STRUCTURE 2aq4

Ternary complex of the catalytic core of REV1 with DNA and dCTP.

Template:ABSTRACT PUBMED 16195463

About this Structure

2AQ4 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Rev1 employs a novel mechanism of DNA synthesis using a protein template., Nair DT, Johnson RE, Prakash L, Prakash S, Aggarwal AK, Science. 2005 Sep 30;309(5744):2219-22. PMID:16195463

Page seeded by OCA on Sun Jul 27 20:57:11 2008

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