1yjm

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 4: Line 4:
|PDB= 1yjm |SIZE=350|CAPTION= <scene name='initialview01'>1yjm</scene>, resolution 2.20&Aring;
|PDB= 1yjm |SIZE=350|CAPTION= <scene name='initialview01'>1yjm</scene>, resolution 2.20&Aring;
|SITE=
|SITE=
-
|LIGAND= <scene name='pdbligand=ACE:ACETYL GROUP'>ACE</scene>
+
|LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene>
-
|ACTIVITY= [http://en.wikipedia.org/wiki/Polynucleotide_5'-hydroxy-kinase Polynucleotide 5'-hydroxy-kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.78 2.7.1.78]
+
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Polynucleotide_5'-hydroxy-kinase Polynucleotide 5'-hydroxy-kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.78 2.7.1.78] </span>
|GENE= Pnk ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
|GENE= Pnk ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
 +
|DOMAIN=
 +
|RELATEDENTRY=[[1yj5|1YJ5]]
 +
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yjm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yjm OCA], [http://www.ebi.ac.uk/pdbsum/1yjm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1yjm RCSB]</span>
}}
}}
Line 36: Line 39:
[[Category: Weinfeld, M.]]
[[Category: Weinfeld, M.]]
[[Category: Williams, R S.]]
[[Category: Williams, R S.]]
-
[[Category: ACE]]
 
[[Category: fha domain]]
[[Category: fha domain]]
[[Category: polynucleotide kinase]]
[[Category: polynucleotide kinase]]
[[Category: xrcc4 phosphopeptide]]
[[Category: xrcc4 phosphopeptide]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:23:46 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:09:46 2008''

Revision as of 22:09, 30 March 2008


PDB ID 1yjm

Drag the structure with the mouse to rotate
, resolution 2.20Å
Ligands: ,
Gene: Pnk (Mus musculus)
Activity: Polynucleotide 5'-hydroxy-kinase, with EC number 2.7.1.78
Related: 1YJ5


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal structure of the FHA domain of mouse polynucleotide kinase in complex with an XRCC4-derived phosphopeptide.


Overview

Mammalian polynucleotide kinase (PNK) is a key component of both the base excision repair (BER) and nonhomologous end-joining (NHEJ) DNA repair pathways. PNK acts as a 5'-kinase/3'-phosphatase to create 5'-phosphate/3'-hydroxyl termini, which are a necessary prerequisite for ligation during repair. PNK is recruited to repair complexes through interactions between its N-terminal FHA domain and phosphorylated components of either pathway. Here, we describe the crystal structure of intact mammalian PNK and a structure of the PNK FHA bound to a cognate phosphopeptide. The kinase domain has a broad substrate binding pocket, which preferentially recognizes double-stranded substrates with recessed 5' termini. In contrast, the phosphatase domain efficiently dephosphorylates single-stranded 3'-phospho termini as well as double-stranded substrates. The FHA domain is linked to the kinase/phosphatase catalytic domain by a flexible tether, and it exhibits a mode of target selection based on electrostatic complementarity between the binding surface and the phosphothreonine peptide.

About this Structure

1YJM is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

The molecular architecture of the mammalian DNA repair enzyme, polynucleotide kinase., Bernstein NK, Williams RS, Rakovszky ML, Cui D, Green R, Karimi-Busheri F, Mani RS, Galicia S, Koch CA, Cass CE, Durocher D, Weinfeld M, Glover JN, Mol Cell. 2005 Mar 4;17(5):657-70. PMID:15749016

Page seeded by OCA on Mon Mar 31 01:09:46 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools