1sn9
From Proteopedia
An Oligomeric Domain-Swapped Beta-Beta-Alpha Mini-Protein
Overview
The x-ray crystal structure of an oligomeric miniprotein has been determined to a 1.2-A resolution by means of multiwavelength anomalous diffraction phasing with selenomethionine analogs that retain the biophysical characteristics of the native peptide. Peptide 1, comprising alpha and beta secondary structure elements with only 21 aa per monomer, associates as a discrete tetramer. The peptide adopts a previously uncharacterized quaternary structure in which alpha and beta components interact to form a tightly packed and well defined hydrophobic core. The structure provides insight into the origins of the unusual thermal stability of the oligomer. The miniprotein shares many characteristics of larger proteins, including cooperative folding, lack of 1-anilino-8-naphthalene sulfonate binding, and limited deuterium exchange, and possesses a buried surface area typical of native proteins.
About this Structure
Full crystallographic information is available from OCA.
Reference
X-ray structure analysis of a designed oligomeric miniprotein reveals a discrete quaternary architecture., Ali MH, Peisach E, Allen KN, Imperiali B, Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12183-8. Epub 2004 Aug 9. PMID:15302930 Page seeded by OCA on Sat May 3 08:54:59 2008
