X-ray structure analysis of a designed oligomeric miniprotein reveals a discrete quaternary architecture.

Abstract:

: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.

authors

Ali MH,Peisach E,Allen KN,Imperiali B

doi

10.1073/pnas.0401245101

keywords:

subject

Has Abstract

pub_date

2004-08-17 00:00:00

pages

12183-8

issue

33

eissn

0027-8424

issn

1091-6490

pii

0401245101

journal_volume

101

pub_type

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