Crystal structure of the GTPase domain of rat dynamin 1

Thomas F. Reubold; Susanne Eschenburg; Andreas Becker; Marilyn Leonard; Sandra L. Schmid; Richard B. Vallee; F. Jon Kull; Dietmar J. Manstein

doi:10.1073/pnas.0506491102

Crystal structure of the GTPase domain of rat dynamin 1

Thomas F. Reubold, Susanne Eschenburg, Andreas Becker, Marilyn Leonard, Sandra L. Schmid, Richard B. Vallee, F. Jon Kull, Dietmar J. Manstein

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

58 Scopus citations

Abstract

Here, we present the 1.9-Å crystal structure of the nucleotide-free GTPase domain of dynamin 1 from Rattus norvegicus. The structure corresponds to an extended form of the canonical GTPase fold observed in Ras proteins. Both nucleotide-binding switch motifs are well resolved, adopting conformations that closely resemble a GTP-bound state not previously observed for nucleotide-free GTPases. Two highly conserved arginines, Arg-66 and Arg-67, greatly restrict the mobility of switch I and are ideally positioned to relay information about the nucleotide state to other parts of the protein. Our results support a model in which switch I residue Arg-59 gates GTP binding in an assembly-dependent manner and the GTPase effector domain functions as an assembly-dependent GTPase activating protein in the fashion of RGS-type GAPs.

Original language	English (US)
Pages (from-to)	13093-13098
Number of pages	6
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	102
Issue number	37
DOIs	https://doi.org/10.1073/pnas.0506491102
State	Published - Sep 13 2005

Keywords

Dictyostelium
GTPase activating protein
GTPase effector domain
Myosin
Protein engineering

ASJC Scopus subject areas

General

Access to Document

10.1073/pnas.0506491102

Cite this

@article{ff3a2171236f4dd6b21c05f4a1e276d3,

title = "Crystal structure of the GTPase domain of rat dynamin 1",

abstract = "Here, we present the 1.9-{\AA} crystal structure of the nucleotide-free GTPase domain of dynamin 1 from Rattus norvegicus. The structure corresponds to an extended form of the canonical GTPase fold observed in Ras proteins. Both nucleotide-binding switch motifs are well resolved, adopting conformations that closely resemble a GTP-bound state not previously observed for nucleotide-free GTPases. Two highly conserved arginines, Arg-66 and Arg-67, greatly restrict the mobility of switch I and are ideally positioned to relay information about the nucleotide state to other parts of the protein. Our results support a model in which switch I residue Arg-59 gates GTP binding in an assembly-dependent manner and the GTPase effector domain functions as an assembly-dependent GTPase activating protein in the fashion of RGS-type GAPs.",

keywords = "Dictyostelium, GTPase activating protein, GTPase effector domain, Myosin, Protein engineering",

author = "Reubold, {Thomas F.} and Susanne Eschenburg and Andreas Becker and Marilyn Leonard and Schmid, {Sandra L.} and Vallee, {Richard B.} and Kull, {F. Jon} and Manstein, {Dietmar J.}",

year = "2005",

month = sep,

day = "13",

doi = "10.1073/pnas.0506491102",

language = "English (US)",

volume = "102",

pages = "13093--13098",

journal = "Proceedings of the National Academy of Sciences of the United States of America",

issn = "0027-8424",

publisher = "National Academy of Sciences",

number = "37",

}

TY - JOUR

T1 - Crystal structure of the GTPase domain of rat dynamin 1

AU - Reubold, Thomas F.

AU - Eschenburg, Susanne

AU - Becker, Andreas

AU - Leonard, Marilyn

AU - Schmid, Sandra L.

AU - Vallee, Richard B.

AU - Kull, F. Jon

AU - Manstein, Dietmar J.

PY - 2005/9/13

Y1 - 2005/9/13

N2 - Here, we present the 1.9-Å crystal structure of the nucleotide-free GTPase domain of dynamin 1 from Rattus norvegicus. The structure corresponds to an extended form of the canonical GTPase fold observed in Ras proteins. Both nucleotide-binding switch motifs are well resolved, adopting conformations that closely resemble a GTP-bound state not previously observed for nucleotide-free GTPases. Two highly conserved arginines, Arg-66 and Arg-67, greatly restrict the mobility of switch I and are ideally positioned to relay information about the nucleotide state to other parts of the protein. Our results support a model in which switch I residue Arg-59 gates GTP binding in an assembly-dependent manner and the GTPase effector domain functions as an assembly-dependent GTPase activating protein in the fashion of RGS-type GAPs.

AB - Here, we present the 1.9-Å crystal structure of the nucleotide-free GTPase domain of dynamin 1 from Rattus norvegicus. The structure corresponds to an extended form of the canonical GTPase fold observed in Ras proteins. Both nucleotide-binding switch motifs are well resolved, adopting conformations that closely resemble a GTP-bound state not previously observed for nucleotide-free GTPases. Two highly conserved arginines, Arg-66 and Arg-67, greatly restrict the mobility of switch I and are ideally positioned to relay information about the nucleotide state to other parts of the protein. Our results support a model in which switch I residue Arg-59 gates GTP binding in an assembly-dependent manner and the GTPase effector domain functions as an assembly-dependent GTPase activating protein in the fashion of RGS-type GAPs.

KW - Dictyostelium

KW - GTPase activating protein

KW - GTPase effector domain

KW - Myosin

KW - Protein engineering

UR - http://www.scopus.com/inward/record.url?scp=24944445874&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=24944445874&partnerID=8YFLogxK

U2 - 10.1073/pnas.0506491102

DO - 10.1073/pnas.0506491102

M3 - Article

C2 - 16141317

AN - SCOPUS:24944445874

SN - 0027-8424

VL - 102

SP - 13093

EP - 13098

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 - 37

ER -

Crystal structure of the GTPase domain of rat dynamin 1

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this