We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1a0i

From Proteopedia

Revision as of 09:39, 21 February 2008 by OCA (Talk | contribs)
Jump to: navigation, search

1a0i, resolution 2.6Å

Drag the structure with the mouse to rotate

ATP-DEPENDENT DNA LIGASE FROM BACTERIOPHAGE T7 COMPLEX WITH ATP

Overview

The crystal structure of the ATP-dependent DNA ligase from bacteriophage T7 has been solved at 2.6 A resolution. The protein comprises two domains with a deep cleft running between them. The structure of a complex with ATP reveals that the nucleotide binding pocket is situated on the larger N-terminal domain, at the base of the cleft between the two domains of the enzyme. Comparison of the overall domain structure with that of DNA methyltransferases, coupled with other evidence, suggests that DNA also binds in this cleft. Since this structure is the first of the nucleotidyltransferase superfamily, which includes the eukaryotic mRNA capping enzymes, the relationship between the structure of DNA ligase and that of other nucleotidyltransferases is also discussed.

About this Structure

1A0I is a Single protein structure of sequence from Bacteriophage t7 with as ligand. The following page contains interesting information on the relation of 1A0I with [DNA Ligase]. Active as DNA ligase (ATP), with EC number 6.5.1.1 Full crystallographic information is available from OCA.

Reference

Crystal structure of an ATP-dependent DNA ligase from bacteriophage T7., Subramanya HS, Doherty AJ, Ashford SR, Wigley DB, Cell. 1996 May 17;85(4):607-15. PMID:8653795

Page seeded by OCA on Thu Feb 21 11:39:34 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools