Hyperactive antifreeze proteins from longhorn beetles: Some structural insights

Erlend Kristiansen; Casper Wilkens; Dennis Steven Friis; Anders Blomkild Lorentzen; Håvard Jenssen; Anders Løbner-Olesen; Hans Ramløv

doi:10.1016/j.jinsphys.2012.09.004

Hyperactive antifreeze proteins from longhorn beetles: Some structural insights

Erlend Kristiansen, Casper Wilkens, Dennis Steven Friis, Anders Blomkild Lorentzen, Håvard Jenssen, Anders Løbner-Olesen, Hans Ramløv

33 Citations (Scopus)

Abstract

This study reports on structural characteristics of hyperactive antifreeze proteins (AFPs) from two species of longhorn beetles. In Rhagium mordax, eight unique mRNAs coding for five different mature AFPs were identified from cold-hardy individuals. These AFPs are apparently homologues to a previously characterized AFP from the closely related species Rhagium inquisitor, and consist of six identifiable repeats of a putative ice binding motif TxTxTxT spaced irregularly apart by segments varying in length from 13 to 20 residues. Circular dichroism spectra show that the AFPs from both species have a high content of β-sheet and low levels of α-helix and random coil. Theoretical predictions of residue-specific secondary structure locate these β-sheets within the putative ice-binding motifs and the central parts of the segments separating them, consistent with an overall β-helical structure with the ice-binding motifs stacked in a β-sheet on one side of the coil. Molecular dynamics models based on these findings show that these AFPs would be energetically stable in a β-helical conformation.

Original language	English
Journal	Journal of Insect Physiology
Volume	58
Issue number	11
Pages (from-to)	1502-1510
Number of pages	9
ISSN	0022-1910
DOIs	https://doi.org/10.1016/j.jinsphys.2012.09.004
Publication status	Published - Nov 2012
Externally published	Yes

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10.1016/j.jinsphys.2012.09.004

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title = "Hyperactive antifreeze proteins from longhorn beetles: Some structural insights",

abstract = "This study reports on structural characteristics of hyperactive antifreeze proteins (AFPs) from two species of longhorn beetles. In Rhagium mordax, eight unique mRNAs coding for five different mature AFPs were identified from cold-hardy individuals. These AFPs are apparently homologues to a previously characterized AFP from the closely related species Rhagium inquisitor, and consist of six identifiable repeats of a putative ice binding motif TxTxTxT spaced irregularly apart by segments varying in length from 13 to 20 residues. Circular dichroism spectra show that the AFPs from both species have a high content of β-sheet and low levels of α-helix and random coil. Theoretical predictions of residue-specific secondary structure locate these β-sheets within the putative ice-binding motifs and the central parts of the segments separating them, consistent with an overall β-helical structure with the ice-binding motifs stacked in a β-sheet on one side of the coil. Molecular dynamics models based on these findings show that these AFPs would be energetically stable in a β-helical conformation.",

author = "Erlend Kristiansen and Casper Wilkens and Friis, {Dennis Steven} and Lorentzen, {Anders Blomkild} and H{\aa}vard Jenssen and Anders L{\o}bner-Olesen and Hans Raml{\o}v",

year = "2012",

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doi = "10.1016/j.jinsphys.2012.09.004",

language = "English",

volume = "58",

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T1 - Hyperactive antifreeze proteins from longhorn beetles: Some structural insights

AU - Kristiansen, Erlend

AU - Wilkens, Casper

AU - Friis, Dennis Steven

AU - Lorentzen, Anders Blomkild

AU - Jenssen, Håvard

AU - Løbner-Olesen, Anders

AU - Ramløv, Hans

PY - 2012/11

Y1 - 2012/11

N2 - This study reports on structural characteristics of hyperactive antifreeze proteins (AFPs) from two species of longhorn beetles. In Rhagium mordax, eight unique mRNAs coding for five different mature AFPs were identified from cold-hardy individuals. These AFPs are apparently homologues to a previously characterized AFP from the closely related species Rhagium inquisitor, and consist of six identifiable repeats of a putative ice binding motif TxTxTxT spaced irregularly apart by segments varying in length from 13 to 20 residues. Circular dichroism spectra show that the AFPs from both species have a high content of β-sheet and low levels of α-helix and random coil. Theoretical predictions of residue-specific secondary structure locate these β-sheets within the putative ice-binding motifs and the central parts of the segments separating them, consistent with an overall β-helical structure with the ice-binding motifs stacked in a β-sheet on one side of the coil. Molecular dynamics models based on these findings show that these AFPs would be energetically stable in a β-helical conformation.

AB - This study reports on structural characteristics of hyperactive antifreeze proteins (AFPs) from two species of longhorn beetles. In Rhagium mordax, eight unique mRNAs coding for five different mature AFPs were identified from cold-hardy individuals. These AFPs are apparently homologues to a previously characterized AFP from the closely related species Rhagium inquisitor, and consist of six identifiable repeats of a putative ice binding motif TxTxTxT spaced irregularly apart by segments varying in length from 13 to 20 residues. Circular dichroism spectra show that the AFPs from both species have a high content of β-sheet and low levels of α-helix and random coil. Theoretical predictions of residue-specific secondary structure locate these β-sheets within the putative ice-binding motifs and the central parts of the segments separating them, consistent with an overall β-helical structure with the ice-binding motifs stacked in a β-sheet on one side of the coil. Molecular dynamics models based on these findings show that these AFPs would be energetically stable in a β-helical conformation.

U2 - 10.1016/j.jinsphys.2012.09.004

DO - 10.1016/j.jinsphys.2012.09.004

M3 - Journal article

C2 - 23000739

SN - 0022-1910

VL - 58

SP - 1502

EP - 1510

JO - Journal of Insect Physiology

JF - Journal of Insect Physiology

IS - 11

ER -

Hyperactive antifreeze proteins from longhorn beetles: Some structural insights

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