1mft
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(New page: 200px<br /><applet load="1mft" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mft, resolution 2.50Å" /> '''Crystal Structure Of...)
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Revision as of 02:03, 25 November 2007
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Crystal Structure Of Four-Helix Bundle Model
Overview
Although the analysis and design of turns that connect the strands in, antiparallel beta-hairpins has reached an advanced state, much less is, known concerning turns between antiparallel helices in helical hairpins., We have conducted an analysis of the structures and sequence preferences, of two types of interhelical turns, each of which connects the two helices, by a two-residue linker in an alphaL-beta conformation. Based on this, analysis, it became apparent that the turn introduced into a designed, four-helix bundle protein, DF1, did not occur within an optimal structural, context. DF1 is a dimeric model for the diiron class of proteins. A longer, loop with a beta-alphaR-beta conformation was inserted between two helices, in the protein, and a sequence was chosen to stabilize its conformation., X-ray crystallography and NMR analysis of the protein showed the structure, to be in excellent agreement with design.
About this Structure
1MFT is a Protein complex structure of sequences from Escherichia coli with ZN as ligand. Full crystallographic information is available from OCA.
Reference
Analysis and design of turns in alpha-helical hairpins., Lahr SJ, Engel DE, Stayrook SE, Maglio O, North B, Geremia S, Lombardi A, DeGrado WF, J Mol Biol. 2005 Mar 11;346(5):1441-54. Epub 2005 Jan 13. PMID:15713492
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