1mow: Difference between revisions

Revision as of 00:36, 3 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:1mow.png

Template:STRUCTURE 1mow

E-DreIE-DreI

Template:ABSTRACT PUBMED 12419232

About this StructureAbout this Structure

1MOW is a Single protein structure of sequence from Desulfurococcus mobilis and chlamydomonas reinhardtii. Full crystallographic information is available from OCA.

ReferenceReference

Design, activity, and structure of a highly specific artificial endonuclease., Chevalier BS, Kortemme T, Chadsey MS, Baker D, Monnat RJ, Stoddard BL, Mol Cell. 2002 Oct;10(4):895-905. PMID:12419232

Page seeded by OCA on Thu Jul 3 00:36:52 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1mow.gif|left|200px]]
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-'''E-DreI'''
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-==Overview==
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-We have generated an artificial highly specific endonuclease by fusing domains of homing endonucleases I-DmoI and I-CreI and creating a new 1400 A(2) protein interface between these domains. Protein engineering was accomplished by combining computational redesign and an in vivo protein-folding screen. The resulting enzyme, E-DreI (Engineered I-DmoI/I-CreI), binds a long chimeric DNA target site with nanomolar affinity, cleaving it precisely at a rate equivalent to its natural parents. The structure of an E-DreI/DNA complex demonstrates the accuracy of the protein interface redesign algorithm and reveals how catalytic function is maintained during the creation of the new endonuclease. These results indicate that it may be possible to generate novel highly specific DNA binding proteins from homing endonucleases.
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