2faq: Difference between revisions
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|PDB= 2faq |SIZE=350|CAPTION= <scene name='initialview01'>2faq</scene>, resolution 1.90Å | |PDB= 2faq |SIZE=350|CAPTION= <scene name='initialview01'>2faq</scene>, resolution 1.90Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[2fao|2FAO]], [[2far|2FAR]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2faq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2faq OCA], [http://www.ebi.ac.uk/pdbsum/2faq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2faq RCSB]</span> | |||
}} | }} | ||
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[[Category: Wang, L K.]] | [[Category: Wang, L K.]] | ||
[[Category: Zhu, H.]] | [[Category: Zhu, H.]] | ||
[[Category: atp]] | [[Category: atp]] | ||
[[Category: ligase]] | [[Category: ligase]] | ||
| Line 38: | Line 38: | ||
[[Category: primase]] | [[Category: primase]] | ||
''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 03:00:11 2008'' | ||
Revision as of 03:00, 31 March 2008
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| , resolution 1.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Related: | 2FAO, 2FAR
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of Pseudomonas aeruginosa LigD polymerase domain with ATP and Manganese
OverviewOverview
DNA ligase D (LigD) is a large polyfunctional protein that participates in a recently discovered pathway of nonhomologous end-joining in bacteria. LigD consists of an ATP-dependent ligase domain fused to a polymerase domain (Pol) and a phosphoesterase module. The Pol activity is remarkable for its dependence on manganese, its ability to perform templated and nontemplated primer extension reactions, and its preference for adding ribonucleotides to blunt DNA ends. Here we report the 1.5-A crystal structure of the Pol domain of Pseudomonas LigD and its complexes with manganese and ATP/dATP substrates, which reveal a minimized polymerase with a two-metal mechanism and a fold similar to that of archaeal DNA primase. Mutational analysis highlights the functionally relevant atomic contacts in the active site. Although distinct nucleoside conformations and contacts for ATP versus dATP are observed in the cocrystals, the functional analysis suggests that the ATP-binding mode is the productive conformation for dNMP and rNMP incorporation. We find that a mutation of Mycobacterium LigD that uniquely ablates the polymerase activity results in increased fidelity of blunt-end double-strand break repair in vivo by virtue of eliminating nucleotide insertions at the recombination junctions. Thus, LigD Pol is a direct catalyst of mutagenic nonhomologous end-joining in vivo. Our studies underscore a previously uncharacterized role for the primase-like polymerase family in DNA repair.
About this StructureAbout this Structure
2FAQ is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.
ReferenceReference
Atomic structure and nonhomologous end-joining function of the polymerase component of bacterial DNA ligase D., Zhu H, Nandakumar J, Aniukwu J, Wang LK, Glickman MS, Lima CD, Shuman S, Proc Natl Acad Sci U S A. 2006 Feb 7;103(6):1711-6. Epub 2006 Jan 30. PMID:16446439
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