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2AQ4

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

Summary for 2AQ4
Entry DOI10.2210/pdb2aq4/pdb
Descriptor5'-D(*AP*TP*CP*CP*TP*CP*CP*CP*CP*TP*AP*C)-3', 5'-D(*TP*AP*AP*GP*GP*TP*AP*GP*GP*GP*GP*AP*GP*GP*AP*T)-3', DNA repair protein REV1, ... (6 entities in total)
Functional Keywordsrev1, polymerase, pad, n-digit, g-loop, transferase
Biological sourceSaccharomyces cerevisiae (baker's yeast)
Cellular locationNucleus: P12689
Total number of polymer chains3
Total formula weight58538.34
Authors
Nair, D.T.,Johnson, R.E.,Prakash, L.,Prakash, S.,Aggarwal, A.K. (deposition date: 2005-08-17, release date: 2005-10-04, Last modification date: 2024-02-14)
Primary citationNair, D.T.,Johnson, R.E.,Prakash, L.,Prakash, S.,Aggarwal, A.K.
Rev1 employs a novel mechanism of DNA synthesis using a protein template.
Science, 309:2219-2222, 2005
Cited by
PubMed Abstract: 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.
PubMed: 16195463
DOI: 10.1126/science.1116336
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.32 Å)
Structure validation

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