2owo
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 2owo |SIZE=350|CAPTION= <scene name='initialview01'>2owo</scene>, resolution 2.300Å | |PDB= 2owo |SIZE=350|CAPTION= <scene name='initialview01'>2owo</scene>, resolution 2.300Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=DA:2'-DEOXYADENOSINE-5'-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2'-DEOXYGUANOSINE-5'-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5'-MONOPHOSPHATE'>DT</scene>, <scene name='pdbligand=OMC:O2'-METHYLYCYTIDINE-5'-MONOPHOSPHATE'>OMC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= ligA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= ligA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2owo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2owo OCA], [http://www.ebi.ac.uk/pdbsum/2owo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2owo RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Nandakumar, J.]] | [[Category: Nandakumar, J.]] | ||
[[Category: Shuman, S.]] | [[Category: Shuman, S.]] | ||
| - | [[Category: AMP]] | ||
| - | [[Category: SO4]] | ||
| - | [[Category: ZN]] | ||
[[Category: dna]] | [[Category: dna]] | ||
[[Category: ligase]] | [[Category: ligase]] | ||
[[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 Mon Mar 31 04:24:15 2008'' |
Revision as of 01:24, 31 March 2008
| |||||||
| , resolution 2.300Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , , , , | ||||||
| Gene: | ligA (Escherichia coli) | ||||||
| Activity: | DNA ligase (NAD(+)), with EC number 6.5.1.2 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Mon Mar 31 04:24:15 2008
