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Comparative structu...
Comparative structural analysis provides new insights into the function of R2-like ligand-binding oxidase
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- Diamanti, Riccardo (author)
- Stockholms universitet,Institutionen för biokemi och biofysik,Department of Biochemistry and Biophysics Stockholm University SE-106 91 Stockholm Sweden
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- Srinivas, Vivek, 1988- (author)
- Stockholms universitet,Institutionen för biokemi och biofysik,Department of Biochemistry and Biophysics Stockholm University SE-106 91 Stockholm Sweden
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- Johansson, Annika I. (author)
- Umeå universitet,Institutionen för fysiologisk botanik,Swedish Metabolomics Center (SMC) SE-907 36 Umeå Sweden
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- Nordström, Anders (author)
- Umeå universitet,Institutionen för fysiologisk botanik,Swedish Metabolomics Center (SMC) SE-907 36 Umeå Sweden
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- Griese, Julia J. (author)
- Uppsala universitet,Strukturbiologi
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- Lebrette, Hugo (author)
- Stockholms universitet,Institutionen för biokemi och biofysik,Department of Biochemistry and Biophysics Stockholm University SE-106 91 Stockholm Sweden; Laboratoire de Microbiologie et Génétique Moléculaires (LMGM) Centre de Biologie Intégrative (CBI) Université de Toulouse CNRS UPS 31062 Toulouse France
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- Högbom, Martin (author)
- Stockholms universitet,Institutionen för biokemi och biofysik,Department of Biochemistry and Biophysics Stockholm University SE‐106 91 Stockholm Sweden
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(creator_code:org_t)
- 2022-03-04
- 2022
- English.
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In: FEBS Letters. - : John Wiley & Sons. - 0014-5793 .- 1873-3468. ; 596:12, s. 1600-1610
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Abstract
Subject headings
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- R2-like ligand-binding oxidase (R2lox) is a ferritin-like protein that harbours a heterodinuclear manganese–iron active site. Although R2lox function is yet to be established, the enzyme binds a fatty acid ligand coordinating the metal centre and catalyses the formation of a tyrosine–valine ether cross-link in the protein scaffold upon O2 activation. Here, we characterized the ligands copurified with R2lox by mass spectrometry-based metabolomics. Moreover, we present the crystal structures of two new homologs of R2lox, from Saccharopolyspora erythraea and Sulfolobus acidocaldarius, at 1.38 Å and 2.26 Å resolution, respectively, providing the highest resolution structure for R2lox, as well as new insights into putative mechanisms regulating the function of the enzyme.
Subject headings
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
- NATURVETENSKAP -- Biologi -- Strukturbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Structural Biology (hsv//eng)
- NATURVETENSKAP -- Biologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences (hsv//eng)
Keyword
- aldehyde deformylating oxygenase
- ferritin-like protein
- hydroxy fatty acids
- long-chain fatty acids
- R2-like ligand-binding oxidase
- R2lox
Publication and Content Type
- ref (subject category)
- art (subject category)
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