X-ray structure analysis of a designed oligomeric miniprotein reveals a discrete quaternary architecture
AUTOR(ES)
Ali, Mayssam H.
FONTE
National Academy of Sciences
RESUMO
The x-ray crystal structure of an oligomeric miniprotein has been determined to a 1.2-Å resolution by means of multiwavelength anomalous diffraction phasing with selenomethionine analogs that retain the biophysical characteristics of the native peptide. Peptide 1, comprising α and β secondary structure elements with only 21 aa per monomer, associates as a discrete tetramer. The peptide adopts a previously uncharacterized quaternary structure in which α and β 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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=514454Documentos Relacionados
- Architecture and Selectivity in Aquaporins: 2.5 Å X-Ray Structure of Aquaporin Z
- Chromosome Structure X. an X-Ray Experiment
- X-RAY ANALYSIS OF RETINAL PHOTORECEPTORS*
- X-ray structure of nucleoside diphosphate kinase.
- Iron distances in hemoglobin: comparison of x-ray crystallographic and extended x-ray absorption fine structure studies.
