Metal Response in Cupriavidus metallidurans, Volume II: Insights into the Structure-Function Relationship of Proteins

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Metal Response in Cupriavidus metallidurans, Volume II: Insights into the Structure-Function Relationship of Proteins. / Vandenbussche, Guy; Mergeay, Max; Van Houdt, Rob.

1 ed. Switzerland : Springer, 2015. 70 p. (SpringerBriefs in Biometals).

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@book{29de05fed7634d43aefc3d86a2602da0,
title = "Metal Response in Cupriavidus metallidurans, Volume II: Insights into the Structure-Function Relationship of Proteins",
abstract = "Bacteria such as Cupriavidus metallidurans have developed different strategies for tolerating toxic levels of metal ions. Metal ion resistance requires the contribution of multiple layers of mechanisms, the most efficient being the efflux of the noxious cations out of the cell regulated by transport systems. Structural and functional data from bacterial primary and secondary transporters are outlined and detailed for the corresponding C. metallidurans proteins. Next, the available high-resolution threedimensional structures of C. metallidurans proteins involved in metal resistance mechanisms are reviewed and their structure-function relationship is discussed.",
keywords = "Anti-sigma factor, Cation diffusion facilitator, Chemiosmotic efflux system, Major facilitator superfamily, Membrane fusion protein, Metal ion efflux, P-type ATPase, Resistance nodulation cell division",
author = "Guy Vandenbussche and Max Mergeay and {Van Houdt}, Rob",
note = "Score = 30",
year = "2015",
month = "7",
language = "English",
isbn = "978-3-319-20623-3",
series = "SpringerBriefs in Biometals",
publisher = "Springer",
edition = "1",

}

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TY - BOOK

T1 - Metal Response in Cupriavidus metallidurans, Volume II: Insights into the Structure-Function Relationship of Proteins

AU - Vandenbussche, Guy

AU - Mergeay, Max

AU - Van Houdt, Rob

N1 - Score = 30

PY - 2015/7

Y1 - 2015/7

N2 - Bacteria such as Cupriavidus metallidurans have developed different strategies for tolerating toxic levels of metal ions. Metal ion resistance requires the contribution of multiple layers of mechanisms, the most efficient being the efflux of the noxious cations out of the cell regulated by transport systems. Structural and functional data from bacterial primary and secondary transporters are outlined and detailed for the corresponding C. metallidurans proteins. Next, the available high-resolution threedimensional structures of C. metallidurans proteins involved in metal resistance mechanisms are reviewed and their structure-function relationship is discussed.

AB - Bacteria such as Cupriavidus metallidurans have developed different strategies for tolerating toxic levels of metal ions. Metal ion resistance requires the contribution of multiple layers of mechanisms, the most efficient being the efflux of the noxious cations out of the cell regulated by transport systems. Structural and functional data from bacterial primary and secondary transporters are outlined and detailed for the corresponding C. metallidurans proteins. Next, the available high-resolution threedimensional structures of C. metallidurans proteins involved in metal resistance mechanisms are reviewed and their structure-function relationship is discussed.

KW - Anti-sigma factor

KW - Cation diffusion facilitator

KW - Chemiosmotic efflux system

KW - Major facilitator superfamily

KW - Membrane fusion protein

KW - Metal ion efflux

KW - P-type ATPase

KW - Resistance nodulation cell division

UR - http://ecm.sckcen.be/OTCS/llisapi.dll/open/ezp_140222

UR - http://knowledgecentre.sckcen.be/so2/bibref/12872

M3 - Book as author

SN - 978-3-319-20623-3

T3 - SpringerBriefs in Biometals

BT - Metal Response in Cupriavidus metallidurans, Volume II: Insights into the Structure-Function Relationship of Proteins

PB - Springer

CY - Switzerland

ER -

ID: 314284