1kdh: Difference between revisions

Revision as of 10:10, 2 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1kdh.png

Template:STRUCTURE 1kdh

Binary Complex of Murine Terminal Deoxynucleotidyl Transferase with a Primer Single Stranded DNABinary Complex of Murine Terminal Deoxynucleotidyl Transferase with a Primer Single Stranded DNA

Template:ABSTRACT PUBMED 11823435

About this StructureAbout this Structure

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

ReferenceReference

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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OCA

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-'''Binary Complex of Murine Terminal Deoxynucleotidyl Transferase with a Primer Single Stranded DNA'''
+===Binary Complex of Murine Terminal Deoxynucleotidyl Transferase with a Primer Single Stranded DNA===
-==Overview==
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-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11823435}}, adds the Publication Abstract to the page
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 [[Category: Nucleotidyl transferase]]
 [[Category: Polymerase]]
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