Quantitative Structural Analysis of Importin-beta Flexibility: Paradigm for Solenoid Protein Structures

Jade K. Forwood; Allison Lange; Ulrich Zachariae; Mary Marfori; Callie Preast; Helmut Grubmueller; Murray Stewart; Anita H. Corbett; Bostjan Kobe

doi:10.1016/j.str.2010.06.015

Quantitative Structural Analysis of Importin-beta Flexibility: Paradigm for Solenoid Protein Structures

Jade K. Forwood, Allison Lange, Ulrich Zachariae, Mary Marfori, Callie Preast, Helmut Grubmueller, Murray Stewart, Anita H. Corbett, Bostjan Kobe

School of Physics and Astronomy

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

Abstract / Description of output

The structure of solenoid proteins facilitates a higher degree of flexibility than most folded proteins. In importin-beta, a nuclear import factor built from 19 tandem HEAT repeats, flexibility plays a crucial role in allowing interactions with a range of different partners. We present a comprehensive analysis of importin-beta flexibility based on a number of different approaches. We determined the crystal structure of unliganded Saccharomyces cerevisiae importin-beta (Kap95) to allow a quantitative comparison with importin-beta bound to different partners. Complementary mutagenesis, small angle X-ray scattering and molecular dynamics studies suggest that the protein samples several conformations in solution. The analyses suggest the flexibility of the solenoid is generated by cumulative small movements along its length. Importin-beta illustrates how solenoid proteins can orchestrate protein interactions in many cellular pathways.

Original language	English
Pages (from-to)	1171-1183
Number of pages	13
Journal	Structure
Volume	18
Issue number	9
DOIs	https://doi.org/10.1016/j.str.2010.06.015
Publication status	Published - 8 Sept 2010

Keywords / Materials (for Non-textual outputs)

NUCLEAR-LOCALIZATION SIGNAL
SCATTERING DATA-ANALYSIS
SACCHAROMYCES-CEREVISIAE
NUCLEOCYTOPLASMIC TRANSPORT
CRYSTAL-STRUCTURE
MOLECULAR-BASIS
EXPORT COMPLEX
RECOGNITION
BINDING
HEAT

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@article{b2241060af0545ebba670bcbee2e44f3,

title = "Quantitative Structural Analysis of Importin-beta Flexibility: Paradigm for Solenoid Protein Structures",

abstract = "The structure of solenoid proteins facilitates a higher degree of flexibility than most folded proteins. In importin-beta, a nuclear import factor built from 19 tandem HEAT repeats, flexibility plays a crucial role in allowing interactions with a range of different partners. We present a comprehensive analysis of importin-beta flexibility based on a number of different approaches. We determined the crystal structure of unliganded Saccharomyces cerevisiae importin-beta (Kap95) to allow a quantitative comparison with importin-beta bound to different partners. Complementary mutagenesis, small angle X-ray scattering and molecular dynamics studies suggest that the protein samples several conformations in solution. The analyses suggest the flexibility of the solenoid is generated by cumulative small movements along its length. Importin-beta illustrates how solenoid proteins can orchestrate protein interactions in many cellular pathways.",

keywords = "NUCLEAR-LOCALIZATION SIGNAL, SCATTERING DATA-ANALYSIS, SACCHAROMYCES-CEREVISIAE, NUCLEOCYTOPLASMIC TRANSPORT, CRYSTAL-STRUCTURE, MOLECULAR-BASIS, EXPORT COMPLEX, RECOGNITION, BINDING, HEAT",

author = "Forwood, {Jade K.} and Allison Lange and Ulrich Zachariae and Mary Marfori and Callie Preast and Helmut Grubmueller and Murray Stewart and Corbett, {Anita H.} and Bostjan Kobe",

year = "2010",

month = sep,

day = "8",

doi = "10.1016/j.str.2010.06.015",

language = "English",

volume = "18",

pages = "1171--1183",

journal = "Structure",

issn = "1878-4186",

publisher = "Cell Press",

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TY - JOUR

T1 - Quantitative Structural Analysis of Importin-beta Flexibility: Paradigm for Solenoid Protein Structures

AU - Forwood, Jade K.

AU - Lange, Allison

AU - Zachariae, Ulrich

AU - Marfori, Mary

AU - Preast, Callie

AU - Grubmueller, Helmut

AU - Stewart, Murray

AU - Corbett, Anita H.

AU - Kobe, Bostjan

PY - 2010/9/8

Y1 - 2010/9/8

N2 - The structure of solenoid proteins facilitates a higher degree of flexibility than most folded proteins. In importin-beta, a nuclear import factor built from 19 tandem HEAT repeats, flexibility plays a crucial role in allowing interactions with a range of different partners. We present a comprehensive analysis of importin-beta flexibility based on a number of different approaches. We determined the crystal structure of unliganded Saccharomyces cerevisiae importin-beta (Kap95) to allow a quantitative comparison with importin-beta bound to different partners. Complementary mutagenesis, small angle X-ray scattering and molecular dynamics studies suggest that the protein samples several conformations in solution. The analyses suggest the flexibility of the solenoid is generated by cumulative small movements along its length. Importin-beta illustrates how solenoid proteins can orchestrate protein interactions in many cellular pathways.

AB - The structure of solenoid proteins facilitates a higher degree of flexibility than most folded proteins. In importin-beta, a nuclear import factor built from 19 tandem HEAT repeats, flexibility plays a crucial role in allowing interactions with a range of different partners. We present a comprehensive analysis of importin-beta flexibility based on a number of different approaches. We determined the crystal structure of unliganded Saccharomyces cerevisiae importin-beta (Kap95) to allow a quantitative comparison with importin-beta bound to different partners. Complementary mutagenesis, small angle X-ray scattering and molecular dynamics studies suggest that the protein samples several conformations in solution. The analyses suggest the flexibility of the solenoid is generated by cumulative small movements along its length. Importin-beta illustrates how solenoid proteins can orchestrate protein interactions in many cellular pathways.

KW - NUCLEAR-LOCALIZATION SIGNAL

KW - SCATTERING DATA-ANALYSIS

KW - SACCHAROMYCES-CEREVISIAE

KW - NUCLEOCYTOPLASMIC TRANSPORT

KW - CRYSTAL-STRUCTURE

KW - MOLECULAR-BASIS

KW - EXPORT COMPLEX

KW - RECOGNITION

KW - BINDING

KW - HEAT

U2 - 10.1016/j.str.2010.06.015

DO - 10.1016/j.str.2010.06.015

M3 - Article

SN - 1878-4186

VL - 18

SP - 1171

EP - 1183

JO - Structure

JF - Structure

IS - 9

ER -

Quantitative Structural Analysis of Importin-beta Flexibility: Paradigm for Solenoid Protein Structures

Abstract / Description of output

Keywords / Materials (for Non-textual outputs)

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