Quaternary structure analyses of an essential oligomeric enzyme

Tatiana P. Soares da Costa; Janni B. Christensen; Sebastien Desbois; Shane E. Gordon; Ruchi Gupta; Campbell J. Hogan; Tao G. Nelson; Matthew T. Downton; Chamodi K. Gardhi; Belinda M. Abbott; John Wagner; Santosh Panjikar; Matthew A. Perugini

doi:10.1016/bs.mie.2015.06.020

Quaternary structure analyses of an essential oligomeric enzyme

Tatiana P. Soares da Costa, Janni B. Christensen, Sebastien Desbois, Shane E. Gordon, Ruchi Gupta, Campbell J. Hogan, Tao G. Nelson, Matthew T. Downton, Chamodi K. Gardhi, Belinda M. Abbott, John Wagner, Santosh Panjikar, Matthew A. Perugini

Biochemistry & Molecular Biology

Research output: Chapter in Book/Report/Conference proceeding › Chapter (Book) › Other › peer-review

20 Citations (Scopus)

Abstract

Here, we review recent studies aimed at defining the importance of quaternary structureto a model oligomeric enzyme, dihydrodipicolinate synthase. This will illustrate thecomplementary and synergistic outcomes of coupling the techniques of analytical ultracentrifugationwith enzyme kinetics, in vitro mutagenesis, macromolecular crystallography,small angle X-ray scattering, and molecular dynamics simulations, to demonstratethe role of subunit self-association in facilitating protein dynamics and enzyme function.This multitechnique approach has yielded new insights into the molecular evolution ofprotein quaternary structure.

Original language	English
Title of host publication	Methods in enzymology
Subtitle of host publication	Analytical ultracentrifugation
Editors	John N. Abelson, Melvin I. Simon, Anna Marie Pyle, David W. Christianson
Place of Publication	New York
Publisher	Academic Press
Pages	205-223
Number of pages	19
Volume	562
ISBN (Print)	9780128029084
DOIs	https://doi.org/10.1016/bs.mie.2015.06.020
Publication status	Published - 2015

Keywords

analytical ultracentrifugation
dihydrodipicolinate synthase
molecular dynamics simulations
oligomer
quaternary structure
self-association
sedimentation equilibrium
sedimentation velocity
small angle x-ray scattering
x-ray crystallography

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10.1016/bs.mie.2015.06.020

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Soares da Costa, T. P., Christensen, J. B., Desbois, S., Gordon, S. E., Gupta, R., Hogan, C. J., Nelson, T. G., Downton, M. T., Gardhi, C. K., Abbott, B. M., Wagner, J., Panjikar, S., & Perugini, M. A. (2015). Quaternary structure analyses of an essential oligomeric enzyme. In J. N. Abelson, M. I. Simon, A. M. Pyle, & D. W. Christianson (Eds.), Methods in enzymology: Analytical ultracentrifugation (Vol. 562, pp. 205-223). Academic Press. https://doi.org/10.1016/bs.mie.2015.06.020

@inbook{7ec14158b32842ef9271e68f508c90d9,

title = "Quaternary structure analyses of an essential oligomeric enzyme",

abstract = "Here, we review recent studies aimed at defining the importance of quaternary structureto a model oligomeric enzyme, dihydrodipicolinate synthase. This will illustrate thecomplementary and synergistic outcomes of coupling the techniques of analytical ultracentrifugationwith enzyme kinetics, in vitro mutagenesis, macromolecular crystallography,small angle X-ray scattering, and molecular dynamics simulations, to demonstratethe role of subunit self-association in facilitating protein dynamics and enzyme function.This multitechnique approach has yielded new insights into the molecular evolution ofprotein quaternary structure.",

keywords = "analytical ultracentrifugation, dihydrodipicolinate synthase, molecular dynamics simulations, oligomer, quaternary structure, self-association, sedimentation equilibrium, sedimentation velocity, small angle x-ray scattering, x-ray crystallography",

author = "{Soares da Costa}, {Tatiana P.} and Christensen, {Janni B.} and Sebastien Desbois and Gordon, {Shane E.} and Ruchi Gupta and Hogan, {Campbell J.} and Nelson, {Tao G.} and Downton, {Matthew T.} and Gardhi, {Chamodi K.} and Abbott, {Belinda M.} and John Wagner and Santosh Panjikar and Perugini, {Matthew A.}",

year = "2015",

doi = "10.1016/bs.mie.2015.06.020",

language = "English",

isbn = "9780128029084",

volume = "562",

pages = "205--223",

editor = "Abelson, {John N. } and Simon, {Melvin I.} and Pyle, {Anna Marie} and Christianson, {David W.}",

booktitle = "Methods in enzymology",

publisher = "Academic Press",

address = "United States of America",

}

Soares da Costa, TP, Christensen, JB, Desbois, S, Gordon, SE, Gupta, R, Hogan, CJ, Nelson, TG, Downton, MT, Gardhi, CK, Abbott, BM, Wagner, J, Panjikar, S & Perugini, MA 2015, Quaternary structure analyses of an essential oligomeric enzyme. in JN Abelson, MI Simon, AM Pyle & DW Christianson (eds), Methods in enzymology: Analytical ultracentrifugation. vol. 562, Academic Press, New York, pp. 205-223. https://doi.org/10.1016/bs.mie.2015.06.020

Quaternary structure analyses of an essential oligomeric enzyme. / Soares da Costa, Tatiana P.; Christensen, Janni B.; Desbois, Sebastien et al.
Methods in enzymology: Analytical ultracentrifugation. ed. / John N. Abelson; Melvin I. Simon; Anna Marie Pyle; David W. Christianson. Vol. 562 New York: Academic Press, 2015. p. 205-223.

Research output: Chapter in Book/Report/Conference proceeding › Chapter (Book) › Other › peer-review

TY - CHAP

T1 - Quaternary structure analyses of an essential oligomeric enzyme

AU - Soares da Costa, Tatiana P.

AU - Christensen, Janni B.

AU - Desbois, Sebastien

AU - Gordon, Shane E.

AU - Gupta, Ruchi

AU - Hogan, Campbell J.

AU - Nelson, Tao G.

AU - Downton, Matthew T.

AU - Gardhi, Chamodi K.

AU - Abbott, Belinda M.

AU - Wagner, John

AU - Panjikar, Santosh

AU - Perugini, Matthew A.

PY - 2015

Y1 - 2015

N2 - Here, we review recent studies aimed at defining the importance of quaternary structureto a model oligomeric enzyme, dihydrodipicolinate synthase. This will illustrate thecomplementary and synergistic outcomes of coupling the techniques of analytical ultracentrifugationwith enzyme kinetics, in vitro mutagenesis, macromolecular crystallography,small angle X-ray scattering, and molecular dynamics simulations, to demonstratethe role of subunit self-association in facilitating protein dynamics and enzyme function.This multitechnique approach has yielded new insights into the molecular evolution ofprotein quaternary structure.

AB - Here, we review recent studies aimed at defining the importance of quaternary structureto a model oligomeric enzyme, dihydrodipicolinate synthase. This will illustrate thecomplementary and synergistic outcomes of coupling the techniques of analytical ultracentrifugationwith enzyme kinetics, in vitro mutagenesis, macromolecular crystallography,small angle X-ray scattering, and molecular dynamics simulations, to demonstratethe role of subunit self-association in facilitating protein dynamics and enzyme function.This multitechnique approach has yielded new insights into the molecular evolution ofprotein quaternary structure.

KW - analytical ultracentrifugation

KW - dihydrodipicolinate synthase

KW - molecular dynamics simulations

KW - oligomer

KW - quaternary structure

KW - self-association

KW - sedimentation equilibrium

KW - sedimentation velocity

KW - small angle x-ray scattering

KW - x-ray crystallography

UR - http://www.ncbi.nlm.nih.gov/pubmed/26412653 or http://www.sciencedirect.com/science/bookseries/00766879/17/part/PA

U2 - 10.1016/bs.mie.2015.06.020

DO - 10.1016/bs.mie.2015.06.020

M3 - Chapter (Book)

SN - 9780128029084

VL - 562

SP - 205

EP - 223

BT - Methods in enzymology

A2 - Abelson, John N.

A2 - Simon, Melvin I.

A2 - Pyle, Anna Marie

A2 - Christianson, David W.

PB - Academic Press

CY - New York

ER -

Quaternary structure analyses of an essential oligomeric enzyme

Abstract

Keywords

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