1vs0

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 4: Line 4:
|PDB= 1vs0 |SIZE=350|CAPTION= <scene name='initialview01'>1vs0</scene>, resolution 2.400&Aring;
|PDB= 1vs0 |SIZE=350|CAPTION= <scene name='initialview01'>1vs0</scene>, resolution 2.400&Aring;
|SITE=
|SITE=
-
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene>
+
|LIGAND= <scene name='pdbligand=APK:5&#39;-O-[(S)-{[(5S)-5-AMINO-6-OXOHEXYL]AMINO}(HYDROXY)PHOSPHORYL]ADENOSINE'>APK</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
|ACTIVITY=
|ACTIVITY=
|GENE= Rv0938, MT0965 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis])
|GENE= Rv0938, MT0965 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis])
 +
|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=PRK08224 ligC], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam04679 DNA_ligase_A_C], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam01068 DNA_ligase_A_M]</span>
 +
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vs0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vs0 OCA], [http://www.ebi.ac.uk/pdbsum/1vs0 PDBsum], [http://www.fli-leibniz.de/cgi-bin/ImgLib.pl?CODE=1kfv JenaLib], [http://www.rcsb.org/pdb/explore.do?structureId=1vs0 RCSB]</span>
}}
}}
Line 29: Line 31:
[[Category: Shuman, S.]]
[[Category: Shuman, S.]]
[[Category: TBSGC, TB Structural Genomics Consortium.]]
[[Category: TBSGC, TB Structural Genomics Consortium.]]
-
[[Category: CL]]
+
[[Category: ligase]]
-
[[Category: MG]]
+
[[Category: nucleotidyl transferase]]
-
[[Category: ZN]]
+
[[Category: ob fold]]
-
[[Category: ligase; ob fold; nucleotidyl transferase]]
+
[[Category: protein structure initiative]]
[[Category: protein structure initiative]]
[[Category: psi]]
[[Category: psi]]
Line 39: Line 40:
[[Category: tbsgc]]
[[Category: tbsgc]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:48:57 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 26 06:10:09 2008''

Revision as of 04:10, 26 March 2008


PDB ID 1vs0

Drag the structure with the mouse to rotate
, resolution 2.400Å
Ligands: , , , ,
Gene: Rv0938, MT0965 (Mycobacterium tuberculosis)
Domains: ligC, DNA_ligase_A_C, DNA_ligase_A_M
Resources: FirstGlance, OCA, PDBsum, JenaLib, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of the Ligase Domain from M. tuberculosis LigD at 2.4A


Overview

DNA ligase D (LigD) is a large polyfunctional enzyme involved in nonhomologous end-joining (NHEJ) in mycobacteria. LigD consists of a C-terminal ATP-dependent ligase domain fused to upstream polymerase and phosphoesterase modules. Here we report the 2.4 angstroms crystal structure of the ligase domain of Mycobacterium LigD, captured as the covalent ligase-AMP intermediate with a divalent metal in the active site. A chloride anion on the protein surface coordinated by the ribose 3'-OH and caged by arginine and lysine side chains is a putative mimetic of the 5'-phosphate at a DNA nick. Structure-guided mutational analysis revealed distinct requirements for the adenylylation and end-sealing reactions catalyzed by LigD. We found that a mutation of Mycobacterium LigD that ablates only ligase activity results in decreased fidelity of NHEJ in vivo and a strong bias of mutagenic events toward deletions instead of insertions at the sealed DNA ends. This phenotype contrasts with the increased fidelity of double-strand break repair in deltaligD cells or in a strain in which only the polymerase function of LigD is defective. We surmise that the signature error-prone quality of bacterial NHEJ in vivo arises from a dynamic balance between the end-remodeling and end-sealing steps.

About this Structure

1VS0 is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

Reference

Crystal structure and nonhomologous end-joining function of the ligase component of Mycobacterium DNA ligase D., Akey D, Martins A, Aniukwu J, Glickman MS, Shuman S, Berger JM, J Biol Chem. 2006 May 12;281(19):13412-23. Epub 2006 Feb 13. PMID:16476729

Page seeded by OCA on Wed Mar 26 06:10:09 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools