1jms
From Proteopedia
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|PDB= 1jms |SIZE=350|CAPTION= <scene name='initialview01'>1jms</scene>, resolution 2.36Å | |PDB= 1jms |SIZE=350|CAPTION= <scene name='initialview01'>1jms</scene>, resolution 2.36Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> | + | |LIGAND= <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= TDT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | |GENE= TDT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY=[[1bpx|1bpx]], [[1bpy|1bpy]], [[1bpz|1bpz]], [[1kan|1kan]], [[1kny|1kny]] | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jms FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jms OCA], [http://www.ebi.ac.uk/pdbsum/1jms PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jms 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 21:35:57 2008'' |
Revision as of 18:35, 30 March 2008
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, resolution 2.36Å | |||||||
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Ligands: | , | ||||||
Gene: | TDT (Mus musculus) | ||||||
Activity: | DNA nucleotidylexotransferase, with EC number 2.7.7.31 | ||||||
Related: | 1bpx, 1bpy, 1bpz, 1kan, 1kny
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Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Crystal Structure of the Catalytic Core of Murine Terminal Deoxynucleotidyl Transferase
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
1JMS 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
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