PRE-driven Protein NMR Structures: an Alternative Approach in Highly Paramagnetic Systems.
Identifieur interne : 000055 ( Main/Exploration ); précédent : 000054; suivant : 000056PRE-driven Protein NMR Structures: an Alternative Approach in Highly Paramagnetic Systems.
Auteurs : Inês B. Trindade [Portugal] ; Michele Invernici [Italie] ; Francesca Cantini [Italie] ; Ricardo O. Louro [Portugal] ; Mario Piccioli [Italie]Source :
- The FEBS journal [ 1742-4658 ] ; 2020.
Abstract
Metalloproteins play key roles across biology, and knowledge of their structure is essential to understand their physiological role. For those metalloproteins containing paramagnetic states, the enhanced relaxation caused by the unpaired electrons often makes signal detection unfeasible near the metal center, precluding adequate structural characterization right where it is more biochemically relevant. Here, we report a protein structure determination by NMR where two different sets of restraints, one containing Nuclear Overhauser Enhancements (NOEs) and another containing Paramagnetic Relaxation Enhancements (PREs), are used separately and eventually together. The protein PioC from Rhodopseudomonas palustris TIE-1 is a High Potential Iron-Sulfur Protein (HiPIP) where the [4Fe-4S] cluster is paramagnetic in both oxidation states at room temperature providing the source of PREs used as alternative distance restraints. Comparison of the family of structures obtained using NOEs only, PREs only and the combination of both reveals that the pairwise root-mean-square deviation (RMSD) between them are similar and comparable with the precision within each family. This demonstrates that, under favorable conditions in terms of protein size and paramagnetic effects, PREs can efficiently complement and eventually replace NOEs for the structural characterization of small paramagnetic metalloproteins and denovo designed metalloproteins by NMR.
DOI: 10.1111/febs.15615
PubMed: 33124176
Affiliations:
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Here, we report a protein structure determination by NMR where two different sets of restraints, one containing Nuclear Overhauser Enhancements (NOEs) and another containing Paramagnetic Relaxation Enhancements (PREs), are used separately and eventually together. The protein PioC from Rhodopseudomonas palustris TIE-1 is a High Potential Iron-Sulfur Protein (HiPIP) where the [4Fe-4S] cluster is paramagnetic in both oxidation states at room temperature providing the source of PREs used as alternative distance restraints. Comparison of the family of structures obtained using NOEs only, PREs only and the combination of both reveals that the pairwise root-mean-square deviation (RMSD) between them are similar and comparable with the precision within each family. This demonstrates that, under favorable conditions in terms of protein size and paramagnetic effects, PREs can efficiently complement and eventually replace NOEs for the structural characterization of small paramagnetic metalloproteins and denovo designed metalloproteins by NMR.</div></front></TEI><pubmed><MedlineCitation Status="Publisher" Owner="NLM"><PMID Version="1">33124176</PMID><DateRevised><Year>2020</Year><Month>10</Month><Day>30</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1742-4658</ISSN><JournalIssue CitedMedium="Internet"><PubDate><Year>2020</Year><Month>Oct</Month><Day>30</Day></PubDate></JournalIssue><Title>The FEBS journal</Title><ISOAbbreviation>FEBS J</ISOAbbreviation></Journal><ArticleTitle>PRE-driven Protein NMR Structures: an Alternative Approach in Highly Paramagnetic Systems.</ArticleTitle><ELocationID EIdType="doi" ValidYN="Y">10.1111/febs.15615</ELocationID><Abstract><AbstractText>Metalloproteins play key roles across biology, and knowledge of their structure is essential to understand their physiological role. For those metalloproteins containing paramagnetic states, the enhanced relaxation caused by the unpaired electrons often makes signal detection unfeasible near the metal center, precluding adequate structural characterization right where it is more biochemically relevant. Here, we report a protein structure determination by NMR where two different sets of restraints, one containing Nuclear Overhauser Enhancements (NOEs) and another containing Paramagnetic Relaxation Enhancements (PREs), are used separately and eventually together. The protein PioC from Rhodopseudomonas palustris TIE-1 is a High Potential Iron-Sulfur Protein (HiPIP) where the [4Fe-4S] cluster is paramagnetic in both oxidation states at room temperature providing the source of PREs used as alternative distance restraints. Comparison of the family of structures obtained using NOEs only, PREs only and the combination of both reveals that the pairwise root-mean-square deviation (RMSD) between them are similar and comparable with the precision within each family. This demonstrates that, under favorable conditions in terms of protein size and paramagnetic effects, PREs can efficiently complement and eventually replace NOEs for the structural characterization of small paramagnetic metalloproteins and denovo designed metalloproteins by NMR.</AbstractText><CopyrightInformation>This article is protected by copyright. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Trindade</LastName><ForeName>Inês B</ForeName><Initials>IB</Initials><AffiliationInfo><Affiliation>Instituto de Tecnologia Química e Biológica António Xavier (ITQB-NOVA), Universidade Nova de Lisboa, Av. da República (EAN), 2780-157, Oeiras, Portugal.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Invernici</LastName><ForeName>Michele</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Magnetic Resonance Center, Department of Chemistry, University of Florence, Via L. Sacconi 6, 50019, Sesto Fiorentino, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cantini</LastName><ForeName>Francesca</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Magnetic Resonance Center, Department of Chemistry, University of Florence, Via L. Sacconi 6, 50019, Sesto Fiorentino, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Louro</LastName><ForeName>Ricardo O</ForeName><Initials>RO</Initials><AffiliationInfo><Affiliation>Instituto de Tecnologia Química e Biológica António Xavier (ITQB-NOVA), Universidade Nova de Lisboa, Av. da República (EAN), 2780-157, Oeiras, Portugal.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Piccioli</LastName><ForeName>Mario</ForeName><Initials>M</Initials><Identifier Source="ORCID">https://orcid.org/0000-0001-9882-9754</Identifier><AffiliationInfo><Affiliation>Magnetic Resonance Center, Department of Chemistry, University of Florence, Via L. 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Trindade</name></noRegion><name sortKey="Louro, Ricardo O" sort="Louro, Ricardo O" uniqKey="Louro R" first="Ricardo O" last="Louro">Ricardo O. Louro</name></country><country name="Italie"><noRegion><name sortKey="Invernici, Michele" sort="Invernici, Michele" uniqKey="Invernici M" first="Michele" last="Invernici">Michele Invernici</name></noRegion><name sortKey="Cantini, Francesca" sort="Cantini, Francesca" uniqKey="Cantini F" first="Francesca" last="Cantini">Francesca Cantini</name><name sortKey="Piccioli, Mario" sort="Piccioli, Mario" uniqKey="Piccioli M" first="Mario" last="Piccioli">Mario Piccioli</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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