2erh
From Proteopedia
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'''Crystal Structure of the E7_G/Im7_G complex; a designed interface between the colicin E7 DNAse and the Im7 immunity protein''' | '''Crystal Structure of the E7_G/Im7_G complex; a designed interface between the colicin E7 DNAse and the Im7 immunity protein''' | ||
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[[Category: Kortemme, T.]] | [[Category: Kortemme, T.]] | ||
[[Category: Stoddard, B L.]] | [[Category: Stoddard, B L.]] | ||
| - | [[Category: | + | [[Category: Computational design]] |
| - | [[Category: | + | [[Category: Hydrogen bond network]] |
| - | [[Category: | + | [[Category: Molecular recognition]] |
| - | [[Category: | + | [[Category: Protein complex]] |
| - | [[Category: | + | [[Category: Redesigned protein-protein interface]] |
| - | [[Category: | + | [[Category: Specificity]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:02:04 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 00:02, 4 May 2008
Crystal Structure of the E7_G/Im7_G complex; a designed interface between the colicin E7 DNAse and the Im7 immunity protein
Overview
The redesign of protein-protein interactions is a stringent test of our understanding of molecular recognition and specificity. Previously we engineered a modest specificity switch into the colicin E7 DNase-Im7 immunity protein complex by identifying mutations that are disruptive in the native complex, but can be compensated by mutations on the interacting partner. Here we extend the approach by systematically sampling alternate rigid body orientations to optimize the interactions in a binding mode specific manner. Using this protocol we designed a de novo hydrogen bond network at the DNase-immunity protein interface and confirmed the design with X-ray crystallographic analysis. Subsequent design of the second shell of interactions guided by insights from the crystal structure on tightly bound water molecules, conformational strain, and packing defects yielded new binding partners that exhibited specificities of at least 300-fold between the cognate and the non-cognate complexes. This multi-step approach should be applicable to the design of polar protein-protein interactions and contribute to the re-engineering of regulatory networks mediated by protein-protein interactions.
About this Structure
2ERH is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Computational design of a new hydrogen bond network and at least a 300-fold specificity switch at a protein-protein interface., Joachimiak LA, Kortemme T, Stoddard BL, Baker D, J Mol Biol. 2006 Aug 4;361(1):195-208. Epub 2006 May 24. PMID:16831445 Page seeded by OCA on Sun May 4 03:02:04 2008
