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dc.contributor.author
Habjanič, Jelena
dc.contributor.author
Chesnov, Serge
dc.contributor.author
Zerbe, Oliver
dc.contributor.author
Freisinger, Eva
dc.date.accessioned
2020-02-07T13:30:27Z
dc.date.available
2020-02-06T04:10:07Z
dc.date.available
2020-02-07T13:30:27Z
dc.date.issued
2020
dc.identifier.issn
1756-5901
dc.identifier.issn
1756-591X
dc.identifier.other
10.1039/c9mt00213h
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/397274
dc.identifier.doi
10.3929/ethz-b-000397274
dc.description.abstract
Metallothioneins (MTs), small cysteine-rich metal-binding proteins, support the viability of organisms under normal physiological conditions and help them to respond to different environmental stressors. Upon metal coordination (e.g. ZnII, CdII, CuI) they form characteristic polynuclear metal–thiolate clusters that are known for their high thermodynamic stability and kinetic lability. However, despite numerous studies, it is still not understood how MTs modulate their metal-binding properties. Pseudomonas MTs are an emerging subclass of bacterial MTs, distinct for their high number of His residues and for several unique features such as an intrinsically disordered long C-terminal tail and multiple variations in the number and nature of coordinating amino acids. These variations might provide the bacteria with a functional advantage derived from evolutionary adaptation to heterogeneous environments. Nearly 90% of the known Pseudomonas MT sequences feature a central YC[C with combining low line]xxC motif, that is altered to YC[S with combining low line]xxC in the rest. We demonstrate that the additional Cys residue serves as a coordinating ligand without influencing the metal-binding capacity, the overall metal-binding stability or the structure. However, the additional ligand changes intra-cluster dynamics and, as a consequence, modulates metal transfer reactions that could be functionally advantageous in vivo.
en_US
dc.format
application/pdf
en_US
dc.language.iso
en
en_US
dc.publisher
Royal Society of Chemistry
en_US
dc.rights.uri
http://creativecommons.org/licenses/by-nc/3.0/
dc.title
Impact of naturally occurring serine/cysteine variations on the structure and function of Pseudomonas metallothioneins
en_US
dc.type
Journal Article
dc.rights.license
Creative Commons Attribution-NonCommercial 3.0 Unported
dc.date.published
2019-11-15
ethz.journal.title
Metallomics
ethz.journal.volume
12
en_US
ethz.journal.issue
1
en_US
ethz.pages.start
23
en_US
ethz.pages.end
33
en_US
ethz.version.deposit
publishedVersion
en_US
ethz.identifier.wos
ethz.identifier.scopus
ethz.publication.place
Cambridge
en_US
ethz.publication.status
published
en_US
ethz.leitzahl
ETH Zürich::00002 - ETH Zürich::00003 - Schulleitung und Dienste::00022 - Bereich VP Forschung / Domain VP Research::02207 - Functional Genomics Center Zurich / Functional Genomics Center Zurich
ethz.leitzahl.certified
ETH Zürich::00002 - ETH Zürich::00003 - Schulleitung und Dienste::00022 - Bereich VP Forschung / Domain VP Research::02207 - Functional Genomics Center Zurich / Functional Genomics Center Zurich
ethz.date.deposited
2020-02-06T04:10:30Z
ethz.source
SCOPUS
ethz.eth
yes
en_US
ethz.availability
Open access
en_US
ethz.rosetta.installDate
2020-02-07T13:30:38Z
ethz.rosetta.lastUpdated
2021-02-15T07:51:43Z
ethz.rosetta.versionExported
true
ethz.COinS
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