1v9p: Difference between revisions

Revision as of 16:32, 21 February 2008

Crystal Structure Of Nad+-Dependent DNA Ligase

OverviewOverview

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 StructureAbout this Structure

1V9P is a Single protein structure of sequence from Thermus filiformis with and as ligands. This structure supersedes 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.

ReferenceReference

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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-[[Image:1v9p.gif|left|200px]]<br /><applet load="1v9p" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1v9p.gif|left|200px]]<br /><applet load="1v9p" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1v9p, resolution 2.90&Aring;" />
 '''Crystal Structure Of Nad+-Dependent DNA Ligase'''<br />
 ==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.
+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==
-V9P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_filiformis Thermus filiformis] with ZN and AMP as [http://en.wikipedia.org/wiki/ligands ligands]. This structure superseeds the now removed PDB entry 1DGT. Active as [http://en.wikipedia.org/wiki/DNA_ligase_(NAD(+)) DNA ligase (NAD(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.5.1.2 6.5.1.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1V9P OCA].
+V9P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_filiformis Thermus filiformis] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=AMP:'>AMP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 1DGT. Active as [http://en.wikipedia.org/wiki/DNA_ligase_(NAD(+)) DNA ligase (NAD(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.5.1.2 6.5.1.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V9P OCA].
 ==Reference==
@@ Line 15: / Line 15: @@
 [[Category: Thermus filiformis]]
 [[Category: Chang, C.]]
-[[Category: Kim, H.K.]]
+[[Category: Kim, H K.]]
-[[Category: Kwon, S.K.]]
+[[Category: Kwon, S K.]]
-[[Category: Lee, J.Y.]]
+[[Category: Lee, J Y.]]
 [[Category: Moon, J.]]
-[[Category: Song, H.K.]]
+[[Category: Song, H K.]]
-[[Category: Suh, S.W.]]
+[[Category: Suh, S W.]]
-[[Category: Yang, J.K.]]
+[[Category: Yang, J K.]]
 [[Category: AMP]]
 [[Category: ZN]]
 [[Category: nad+-dependent dna ligase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:31:54 2007''
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