1yf2

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Template:STRUCTURE 1yf2

Three-dimensional structure of DNA sequence specificity (S) subunit of a type I restriction-modification enzyme and its functional implications

Overview

Type I restriction-modification enzymes are differentiated from type II and type III enzymes by their recognition of two specific dsDNA sequences separated by a given spacer and cleaving DNA randomly away from the recognition sites. They are oligomeric proteins formed by three subunits: a specificity subunit, a methylation subunit, and a restriction subunit. We solved the crystal structure of a specificity subunit from Methanococcus jannaschii at 2.4-A resolution. Two highly conserved regions (CRs) in the middle and at the C terminus form a coiled-coil of long antiparallel alpha-helices. Two target recognition domains form globular structures with almost identical topologies and two separate DNA binding clefts with a modeled DNA helix axis positioned across the CR helices. The structure suggests that the coiled-coil CRs act as a molecular ruler for the separation between two recognized DNA sequences. Furthermore, the relative orientation of the two DNA binding clefts suggests kinking of bound dsDNA and exposing of target adenines from the recognized DNA sequences.

About this Structure

1YF2 is a Single protein structure of sequence from Methanocaldococcus jannaschii dsm 2661. Full crystallographic information is available from OCA.

Reference

Crystal structure of DNA sequence specificity subunit of a type I restriction-modification enzyme and its functional implications., Kim JS, DeGiovanni A, Jancarik J, Adams PD, Yokota H, Kim R, Kim SH, Proc Natl Acad Sci U S A. 2005 Mar 1;102(9):3248-53. Epub 2005 Feb 22. PMID:15728358 Page seeded by OCA on Sat May 3 16:14:38 2008