1b7e: Difference between revisions

Revision as of 18:26, 30 June 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:1b7e.png

Template:STRUCTURE 1b7e

TRANSPOSASE INHIBITORTRANSPOSASE INHIBITOR

Template:ABSTRACT PUBMED 10207011

About this StructureAbout this Structure

1B7E is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

The three-dimensional structure of a Tn5 transposase-related protein determined to 2.9-A resolution., Davies DR, Mahnke Braam L, Reznikoff WS, Rayment I, J Biol Chem. 1999 Apr 23;274(17):11904-13. PMID:10207011

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OCA

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-'''TRANSPOSASE INHIBITOR'''
+===TRANSPOSASE INHIBITOR===
-==Overview==
+<!--
-Transposon Tn5 employs a unique means of self-regulation by expressing a truncated version of the transposase enzyme that acts as an inhibitor. The inhibitor protein differs from the full-length transposase only by the absence of the first 55 N-terminal amino acid residues. It contains the catalytic active site of transposase and a C-terminal domain involved in protein-protein interactions. The three-dimensional structure of Tn5 inhibitor determined to 2.9-A resolution is reported here. A portion of the protein fold of the catalytic core domain is similar to the folds of human immunodeficiency virus-1 integrase, avian sarcoma virus integrase, and bacteriophage Mu transposase. The Tn5 inhibitor contains an insertion that extends the beta-sheet of the catalytic core from 5 to 9 strands. All three of the conserved residues that make up the "DDE" motif of the active site are visible in the structure. An arginine residue that is strictly conserved among the IS4 family of bacterial transposases is present at the center of the active site, suggesting a catalytic motif of "DDRE." A novel C-terminal domain forms a dimer interface across a crystallographic 2-fold axis. Although this dimer represents the structure of the inhibited complex, it provides insight into the structure of the synaptic complex.
+The line below this paragraph, {{ABSTRACT_PUBMED_10207011}}, adds the Publication Abstract to the page
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 ==About this Structure==
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 [[Category: Polynucleotidyl transferase]]
 [[Category: Transposase]]
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