1sn9

An Oligomeric Domain-Swapped Beta-Beta-Alpha Mini-Protein

spinqualitylabelsall models 1sn9, resolution 1.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1sn9 is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.2Å Ligands: ACE, DAL, DBZ, DPR, NH2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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