1kdh
From Proteopedia
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|PDB= 1kdh |SIZE=350|CAPTION= <scene name='initialview01'>1kdh</scene>, resolution 3.00Å | |PDB= 1kdh |SIZE=350|CAPTION= <scene name='initialview01'>1kdh</scene>, resolution 3.00Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> | + | |LIGAND= <scene name='pdbligand=BRU:5-BROMO-2'-DEOXYURIDINE-5'-MONOPHOSPHATE'>BRU</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/DNA_nucleotidylexotransferase DNA nucleotidylexotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.31 2.7.7.31] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_nucleotidylexotransferase DNA nucleotidylexotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.31 2.7.7.31] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1jms|1JMS]], [[1bpy|1BPY]], [[1kej|1KEJ]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kdh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kdh OCA], [http://www.ebi.ac.uk/pdbsum/1kdh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kdh RCSB]</span> | ||
}} | }} | ||
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[[Category: Rougeon, F.]] | [[Category: Rougeon, F.]] | ||
[[Category: Sukumar, N.]] | [[Category: Sukumar, N.]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: NA]] | ||
[[Category: nucleotidyl transferase]] | [[Category: nucleotidyl transferase]] | ||
[[Category: polymerase]] | [[Category: polymerase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:46:58 2008'' |
Revision as of 18:47, 30 March 2008
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| , resolution 3.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Activity: | DNA nucleotidylexotransferase, with EC number 2.7.7.31 | ||||||
| Related: | 1JMS, 1BPY, 1KEJ
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Binary Complex of Murine Terminal Deoxynucleotidyl Transferase with a Primer Single Stranded DNA
Overview
The crystal structure of the catalytic core of murine terminal deoxynucleotidyltransferase (TdT) at 2.35 A resolution reveals a typical DNA polymerase beta-like fold locked in a closed form. In addition, the structures of two different binary complexes, one with an oligonucleotide primer and the other with an incoming ddATP-Co(2+) complex, show that the substrates and the two divalent ions in the catalytic site are positioned in TdT in a manner similar to that described for the human DNA polymerase beta ternary complex, suggesting a common two metal ions mechanism of nucleotidyl transfer in these two proteins. The inability of TdT to accommodate a template strand can be explained by steric hindrance at the catalytic site caused by a long lariat-like loop, which is absent in DNA polymerase beta. However, displacement of this discriminating loop would be sufficient to unmask a number of evolutionarily conserved residues, which could then interact with a template DNA strand. The present structure can be used to model the recently discovered human polymerase mu, with which it shares 43% sequence identity.
About this Structure
1KDH is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Crystal structures of a template-independent DNA polymerase: murine terminal deoxynucleotidyltransferase., Delarue M, Boule JB, Lescar J, Expert-Bezancon N, Jourdan N, Sukumar N, Rougeon F, Papanicolaou C, EMBO J. 2002 Feb 1;21(3):427-39. PMID:11823435
Page seeded by OCA on Sun Mar 30 21:46:58 2008
