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

Mayssam H. Ali; Ezra Peisach; Karen N. Allen; Barbara Imperiali

doi:10.1073/pnas.0401245101

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

Mayssam H. Ali
, Ezra Peisach
, Karen N. Allen
, Barbara Imperiali

Research output: Contribution to journal › Article › peer-review

Abstract

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.

Original language	American English
Pages (from-to)	12183-12188
Number of pages	6
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	101
Issue number	33
DOIs	https://doi.org/10.1073/pnas.0401245101
State	Published - Aug 17 2004
Externally published	Yes

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10.1073/pnas.0401245101

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title = "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-{\AA} 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.",

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T1 - X-ray structure analysis of a designed oligomeric miniprotein reveals a discrete quaternary architecture

AU - Ali, Mayssam H.

AU - Peisach, Ezra

AU - Allen, Karen N.

AU - Imperiali, Barbara

PY - 2004/8/17

Y1 - 2004/8/17

N2 - 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.

AB - 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.

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U2 - 10.1073/pnas.0401245101

DO - 10.1073/pnas.0401245101

M3 - Article

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SN - 0027-8424

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JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

IS - 33

ER -

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

Abstract

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