Structure of a functional amyloid protein subunit computed using sequence variation

Pengfei Tian; Wouter Krogh Boomsma; Yong Wang; Daniel Otzen; Mogens Høgh Jensen; Kresten Lindorff-Larsen

doi:10.1021/ja5093634

Structure of a functional amyloid protein subunit computed using sequence variation

Pengfei Tian, Wouter Krogh Boomsma, Yong Wang, Daniel Otzen, Mogens Høgh Jensen, Kresten Lindorff-Larsen

66 Citationer (Scopus)

Abstract

Functional amyloid fibers, called curli, play a critical role in adhesion and invasion of many bacteria. Unlike pathological amyloids, curli structures are formed by polypeptide sequences whose amyloid structure has been selected for during evolution. This important distinction provides us with an opportunity to obtain structural insights from an unexpected source: the covariation of amino acids in sequences of different curli proteins. We used recently developed methods to extract amino acid contacts from a multiple sequence alignment of homologues of the curli subunit protein, CsgA. Together with an efficient force field, these contacts allow us to determine structural models of CsgA. We find that CsgA forms a β-helical structure, where each turn corresponds to previously identified repeat sequences in CsgA. The proposed structure is validated by previously measured solid-state NMR, electron microscopy, and X-ray diffraction data and agrees with an earlier proposed model derived by complementary means.

Originalsprog	Engelsk
Tidsskrift	Journal of the American Chemical Society
Vol/bind	137
Udgave nummer	1
Sider (fra-til)	22–25
Antal sider	4
ISSN	0002-7863
DOI	https://doi.org/10.1021/ja5093634
Status	Udgivet - 14 jan. 2015

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10.1021/ja5093634

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abstract = "Functional amyloid fibers, called curli, play a critical role in adhesion and invasion of many bacteria. Unlike pathological amyloids, curli structures are formed by polypeptide sequences whose amyloid structure has been selected for during evolution. This important distinction provides us with an opportunity to obtain structural insights from an unexpected source: the covariation of amino acids in sequences of different curli proteins. We used recently developed methods to extract amino acid contacts from a multiple sequence alignment of homologues of the curli subunit protein, CsgA. Together with an efficient force field, these contacts allow us to determine structural models of CsgA. We find that CsgA forms a β-helical structure, where each turn corresponds to previously identified repeat sequences in CsgA. The proposed structure is validated by previously measured solid-state NMR, electron microscopy, and X-ray diffraction data and agrees with an earlier proposed model derived by complementary means.",

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T1 - Structure of a functional amyloid protein subunit computed using sequence variation

AU - Tian, Pengfei

AU - Boomsma, Wouter Krogh

AU - Wang, Yong

AU - Otzen, Daniel

AU - Jensen, Mogens Høgh

AU - Lindorff-Larsen, Kresten

PY - 2015/1/14

Y1 - 2015/1/14

N2 - Functional amyloid fibers, called curli, play a critical role in adhesion and invasion of many bacteria. Unlike pathological amyloids, curli structures are formed by polypeptide sequences whose amyloid structure has been selected for during evolution. This important distinction provides us with an opportunity to obtain structural insights from an unexpected source: the covariation of amino acids in sequences of different curli proteins. We used recently developed methods to extract amino acid contacts from a multiple sequence alignment of homologues of the curli subunit protein, CsgA. Together with an efficient force field, these contacts allow us to determine structural models of CsgA. We find that CsgA forms a β-helical structure, where each turn corresponds to previously identified repeat sequences in CsgA. The proposed structure is validated by previously measured solid-state NMR, electron microscopy, and X-ray diffraction data and agrees with an earlier proposed model derived by complementary means.

AB - Functional amyloid fibers, called curli, play a critical role in adhesion and invasion of many bacteria. Unlike pathological amyloids, curli structures are formed by polypeptide sequences whose amyloid structure has been selected for during evolution. This important distinction provides us with an opportunity to obtain structural insights from an unexpected source: the covariation of amino acids in sequences of different curli proteins. We used recently developed methods to extract amino acid contacts from a multiple sequence alignment of homologues of the curli subunit protein, CsgA. Together with an efficient force field, these contacts allow us to determine structural models of CsgA. We find that CsgA forms a β-helical structure, where each turn corresponds to previously identified repeat sequences in CsgA. The proposed structure is validated by previously measured solid-state NMR, electron microscopy, and X-ray diffraction data and agrees with an earlier proposed model derived by complementary means.

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Structure of a functional amyloid protein subunit computed using sequence variation

Abstract

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