2owo
From Proteopedia
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==Overview== | ==Overview== | ||
| - | NAD(+)-dependent DNA ligases (LigA) are ubiquitous in bacteria and | + | NAD(+)-dependent DNA ligases (LigA) are ubiquitous in bacteria and essential for growth. Their distinctive substrate specificity and domain organization vis-a-vis human ATP-dependent ligases make them outstanding targets for anti-infective drug discovery. We report here the 2.3 A crystal structure of Escherichia coli LigA bound to an adenylylated nick, which captures LigA in a state poised for strand closure and reveals the basis for nick recognition. LigA envelopes the DNA within a protein clamp. Large protein domain movements and remodeling of the active site orchestrate progression through the three chemical steps of the ligation reaction. The structure inspires a strategy for inhibitor design. |
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | Last | + | Last stop on the road to repair: structure of E. coli DNA ligase bound to nicked DNA-adenylate., Nandakumar J, Nair PA, Shuman S, Mol Cell. 2007 Apr 27;26(2):257-71. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17466627 17466627] |
[[Category: DNA ligase (NAD(+))]] | [[Category: DNA ligase (NAD(+))]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Nair, P | + | [[Category: Nair, P A.]] |
[[Category: Nandakumar, J.]] | [[Category: Nandakumar, J.]] | ||
[[Category: Shuman, S.]] | [[Category: Shuman, S.]] | ||
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[[Category: protein/dna complex]] | [[Category: protein/dna complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:23:22 2008'' |
Revision as of 16:23, 21 February 2008
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Last Stop on the Road to Repair: Structure of E.coli DNA Ligase Bound to Nicked DNA-Adenylate
Overview
NAD(+)-dependent DNA ligases (LigA) are ubiquitous in bacteria and essential for growth. Their distinctive substrate specificity and domain organization vis-a-vis human ATP-dependent ligases make them outstanding targets for anti-infective drug discovery. We report here the 2.3 A crystal structure of Escherichia coli LigA bound to an adenylylated nick, which captures LigA in a state poised for strand closure and reveals the basis for nick recognition. LigA envelopes the DNA within a protein clamp. Large protein domain movements and remodeling of the active site orchestrate progression through the three chemical steps of the ligation reaction. The structure inspires a strategy for inhibitor design.
About this Structure
2OWO is a Single protein structure of sequence from Escherichia coli with , and as ligands. Active as DNA ligase (NAD(+)), with EC number 6.5.1.2 Full crystallographic information is available from OCA.
Reference
Last stop on the road to repair: structure of E. coli DNA ligase bound to nicked DNA-adenylate., Nandakumar J, Nair PA, Shuman S, Mol Cell. 2007 Apr 27;26(2):257-71. PMID:17466627
Page seeded by OCA on Thu Feb 21 18:23:22 2008
Categories: DNA ligase (NAD(+)) | Escherichia coli | Single protein | Nair, P A. | Nandakumar, J. | Shuman, S. | AMP | SO4 | ZN | Dna | Ligase | Protein/dna complex
