1v9p
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1v9p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1v9p, resolution 2.90Å" /> '''Crystal Structure Of...)
Next diff →
Revision as of 02:24, 21 November 2007
|
Crystal Structure Of Nad+-Dependent DNA Ligase
Overview
DNA ligases catalyze the crucial step of joining the breaks in duplex DNA, during DNA replication, repair and recombination, utilizing either ATP or, NAD(+) as a cofactor. Despite the difference in cofactor specificity and, limited overall sequence similarity, the two classes of DNA ligase share, basically the same catalytic mechanism. In this study, the crystal, structure of an NAD(+)-dependent DNA ligase from Thermus filiformis, a 667, residue multidomain protein, has been determined by the multiwavelength, anomalous diffraction (MAD) method. It reveals highly modular architecture, and a unique circular arrangement of its four distinct domains. It also, provides clues for protein flexibility and DNA-binding sites. A model for, the multidomain ligase action involving large conformational changes is, proposed.
About this Structure
1V9P is a Single protein structure of sequence from Thermus filiformis with ZN and AMP as ligands. This structure superseeds the now removed PDB entry 1DGT. Active as DNA ligase (NAD(+)), with EC number 6.5.1.2 Full crystallographic information is available from OCA.
Reference
Crystal structure of NAD(+)-dependent DNA ligase: modular architecture and functional implications., Lee JY, Chang C, Song HK, Moon J, Yang JK, Kim HK, Kwon ST, Suh SW, EMBO J. 2000 Mar 1;19(5):1119-29. PMID:10698952
Page seeded by OCA on Wed Nov 21 04:31:54 2007
