1v9p

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{{STRUCTURE_1v9p| PDB=1v9p | SCENE= }}
{{STRUCTURE_1v9p| PDB=1v9p | SCENE= }}
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'''Crystal Structure Of Nad+-Dependent DNA Ligase'''
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===Crystal Structure Of Nad+-Dependent DNA Ligase===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_10698952}}
==About this Structure==
==About this Structure==
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[[Category: Yang, J K.]]
[[Category: Yang, J K.]]
[[Category: Nad+-dependent dna ligase]]
[[Category: Nad+-dependent dna ligase]]
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Revision as of 23:29, 28 July 2008

Image:1v9p.png

Template:STRUCTURE 1v9p

Crystal Structure Of Nad+-Dependent DNA Ligase

Template:ABSTRACT PUBMED 10698952

About this Structure

1V9P is a Single protein structure of sequence from Thermus filiformis. This structure supersedes the now removed PDB entry 1dgt. 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

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