2aq4
From Proteopedia
Ternary complex of the catalytic core of REV1 with DNA and dCTP.
Overview
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.
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 Sat May 3 19:20:02 2008
Categories: Saccharomyces cerevisiae | Single protein | Aggarwal, A K. | Johnson, R E. | Nair, D T. | Prakash, L. | Prakash, S. | G-loop | N-digit | Pad | Polymerase | Rev1
