1kh0
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY=[[1hz5|1HZ5]], [[1hz6|1HZ6]] | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kh0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kh0 OCA], [http://www.ebi.ac.uk/pdbsum/1kh0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kh0 RCSB]</span> | ||
}} | }} | ||
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[[Category: type 1' beta turn]] | [[Category: type 1' beta turn]] | ||
- | ''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 21:48:30 2008'' |
Revision as of 18:48, 30 March 2008
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, resolution 1.90Å | |||||||
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Related: | 1HZ5, 1HZ6
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Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Accurate Computer Base Design of a New Backbone Conformation in the Second Turn of Protein L
Overview
The rational design of loops and turns is a key step towards creating proteins with new functions. We used a computational design procedure to create new backbone conformations in the second turn of protein L. The Protein Data Bank was searched for alternative turn conformations, and sequences optimal for these turns in the context of protein L were identified using a Monte Carlo search procedure and an energy function that favors close packing. Two variants containing 12 and 14 mutations were found to be as stable as wild-type protein L. The crystal structure of one of the variants has been solved at a resolution of 1.9 A, and the backbone conformation in the second turn is remarkably close to that of the in silico model (1.1 A RMSD) while it differs significantly from that of wild-type protein L (the turn residues are displaced by an average of 7.2 A). The folding rates of the redesigned proteins are greater than that of the wild-type protein and in contrast to wild-type protein L the second beta-turn appears to be formed at the rate limiting step in folding.
About this Structure
1KH0 is a Single protein structure of sequence from Finegoldia magna. Full crystallographic information is available from OCA.
Reference
Accurate computer-based design of a new backbone conformation in the second turn of protein L., Kuhlman B, O'Neill JW, Kim DE, Zhang KY, Baker D, J Mol Biol. 2002 Jan 18;315(3):471-7. PMID:11786026
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