The structure and function of antiamoebin I, a proline-rich membrane-active polypeptide

C. F. Snook; G. A. Woolley; G. Oliva; Vasantha Pattabhi; Stephen Paul Wood; T. L. Blundell; B. A. Wallace

doi:10.1016/S0969-2126(98)00079-3

The structure and function of antiamoebin I, a proline-rich membrane-active polypeptide

C. F. Snook, G. A. Woolley, G. Oliva, Vasantha Pattabhi, Stephen Paul Wood, T. L. Blundell, B. A. Wallace

Institute of Life Sciences and Healthcare

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

Abstract

BACKGROUND: Antiamoebin is a member of the peptaibol family of polypeptides and has a unique antibiotic activity: it acts as an antiamoebic agent, but does not effectively haemolyze erythrocytes even though it does exhibit membrane-modifying activity.

RESULTS: The structure of antiamoebin I has been determined by X-ray crystallography at 1.4 A resolution. The molecule forms a helical structure, which, as a result of the presence of a number of proline and hydroxyproline residues, has a deep bend in the middle. Circular dichroism spectroscopy, single-channel conductance studies and fluorescence diffusion studies suggest a mode of ion transport that is entirely different from that of the other two members of the peptaibol family (alamethicin and zervamicin) whose structures and functions have been examined in detail.

CONCLUSIONS: The structure of the polypeptide has been determined and a functional model for its mode of action in membranes is presented. Although under some conditions antiamoebin may form ion channels, unlike the closely related alamethicin and zervamicin polypeptides, its major membrane-modifying activity appears to be as an ion carrier.

Original language	English
Pages (from-to)	783-792
Journal	Structure
Volume	6
Issue number	6
DOIs	https://doi.org/10.1016/S0969-2126(98)00079-3
Publication status	Published - 1 Jun 1998

Keywords

circular dichroism spectroscopy
conductance
crystal structure
ion channels
membrane transport

Access to Document

10.1016/S0969-2126(98)00079-3

Cite this

@article{bbb75865985b446c8724af226b13f4a9,

title = "The structure and function of antiamoebin I, a proline-rich membrane-active polypeptide",

abstract = "BACKGROUND: Antiamoebin is a member of the peptaibol family of polypeptides and has a unique antibiotic activity: it acts as an antiamoebic agent, but does not effectively haemolyze erythrocytes even though it does exhibit membrane-modifying activity.RESULTS: The structure of antiamoebin I has been determined by X-ray crystallography at 1.4 A resolution. The molecule forms a helical structure, which, as a result of the presence of a number of proline and hydroxyproline residues, has a deep bend in the middle. Circular dichroism spectroscopy, single-channel conductance studies and fluorescence diffusion studies suggest a mode of ion transport that is entirely different from that of the other two members of the peptaibol family (alamethicin and zervamicin) whose structures and functions have been examined in detail.CONCLUSIONS: The structure of the polypeptide has been determined and a functional model for its mode of action in membranes is presented. Although under some conditions antiamoebin may form ion channels, unlike the closely related alamethicin and zervamicin polypeptides, its major membrane-modifying activity appears to be as an ion carrier.",

keywords = "circular dichroism spectroscopy, conductance, crystal structure, ion channels, membrane transport",

author = "Snook, {C. F.} and Woolley, {G. A.} and G. Oliva and Vasantha Pattabhi and Wood, {Stephen Paul} and Blundell, {T. L.} and Wallace, {B. A.}",

year = "1998",

month = jun,

day = "1",

doi = "10.1016/S0969-2126(98)00079-3",

language = "English",

volume = "6",

pages = "783--792",

journal = "Structure",

issn = "0969-2126",

publisher = "Cell Press",

number = "6",

}

TY - JOUR

T1 - The structure and function of antiamoebin I, a proline-rich membrane-active polypeptide

AU - Snook, C. F.

AU - Woolley, G. A.

AU - Oliva, G.

AU - Pattabhi, Vasantha

AU - Wood, Stephen Paul

AU - Blundell, T. L.

AU - Wallace, B. A.

PY - 1998/6/1

Y1 - 1998/6/1

N2 - BACKGROUND: Antiamoebin is a member of the peptaibol family of polypeptides and has a unique antibiotic activity: it acts as an antiamoebic agent, but does not effectively haemolyze erythrocytes even though it does exhibit membrane-modifying activity.RESULTS: The structure of antiamoebin I has been determined by X-ray crystallography at 1.4 A resolution. The molecule forms a helical structure, which, as a result of the presence of a number of proline and hydroxyproline residues, has a deep bend in the middle. Circular dichroism spectroscopy, single-channel conductance studies and fluorescence diffusion studies suggest a mode of ion transport that is entirely different from that of the other two members of the peptaibol family (alamethicin and zervamicin) whose structures and functions have been examined in detail.CONCLUSIONS: The structure of the polypeptide has been determined and a functional model for its mode of action in membranes is presented. Although under some conditions antiamoebin may form ion channels, unlike the closely related alamethicin and zervamicin polypeptides, its major membrane-modifying activity appears to be as an ion carrier.

AB - BACKGROUND: Antiamoebin is a member of the peptaibol family of polypeptides and has a unique antibiotic activity: it acts as an antiamoebic agent, but does not effectively haemolyze erythrocytes even though it does exhibit membrane-modifying activity.RESULTS: The structure of antiamoebin I has been determined by X-ray crystallography at 1.4 A resolution. The molecule forms a helical structure, which, as a result of the presence of a number of proline and hydroxyproline residues, has a deep bend in the middle. Circular dichroism spectroscopy, single-channel conductance studies and fluorescence diffusion studies suggest a mode of ion transport that is entirely different from that of the other two members of the peptaibol family (alamethicin and zervamicin) whose structures and functions have been examined in detail.CONCLUSIONS: The structure of the polypeptide has been determined and a functional model for its mode of action in membranes is presented. Although under some conditions antiamoebin may form ion channels, unlike the closely related alamethicin and zervamicin polypeptides, its major membrane-modifying activity appears to be as an ion carrier.

KW - circular dichroism spectroscopy

KW - conductance

KW - crystal structure

KW - ion channels

KW - membrane transport

U2 - 10.1016/S0969-2126(98)00079-3

DO - 10.1016/S0969-2126(98)00079-3

M3 - Article

SN - 0969-2126

VL - 6

SP - 783

EP - 792

JO - Structure

JF - Structure

IS - 6

ER -

The structure and function of antiamoebin I, a proline-rich membrane-active polypeptide

Abstract

Keywords

Access to Document

Fingerprint

Cite this