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Crystallographic bi...
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Sridhar, ShruthiFaculty of Biochemistry and Molecular Medicine, University of Oulu, Oulu, Finland;Biocenter Oulu, University of Oulu, Oulu, Finland
(author)
Crystallographic binding studies of rat peroxisomal multifunctional enzyme type 1 with 3-ketodecanoyl-CoA : capturing active and inactive states of its hydratase and dehydrogenase catalytic sites
- Article/chapterEnglish2020
Publisher, publication year, extent ...
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2020-11-24
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International Union of Crystallography (IUCr),2020
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printrdacarrier
Numbers
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LIBRIS-ID:oai:DiVA.org:uu-455592
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https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-455592URI
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https://doi.org/10.1107/s2059798320013819DOI
Supplementary language notes
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Language:English
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Summary in:English
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Subject category:ref swepub-contenttype
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Subject category:art swepub-publicationtype
Notes
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The peroxisomal multifunctional enzyme type 1 (MFE1) catalyzes two successive reactions in the beta-oxidation cycle: the 2E-enoyl-CoA hydratase (ECH) and NAD(+)-dependent 3S-hydroxyacyl-CoA dehydrogenase (HAD) reactions. MFE1 is a monomeric enzyme that has five domains. The N-terminal part (domains A and B) adopts the crotonase fold and the C-terminal part (domains C, D and E) adopts the HAD fold. A new crystal form of MFE1 has captured a conformation in which both active sites are noncompetent. This structure, at 1.7 angstrom resolution, shows the importance of the interactions between Phe272 in domain B (the linker helix; helix H10 of the crotonase fold) and the beginning of loop 2 (of the crotonase fold) in stabilizing the competent ECH active-site geometry. In addition, protein crystallographic binding studies using optimized crystal-treatment protocols have captured a structure with both the 3-ketodecanoyl-CoA product and NAD(+) bound in the HAD active site, showing the interactions between 3-ketodecanoyl-CoA and residues of the C, D and E domains. Structural comparisons show the importance of domain movements, in particular of the C domain with respect to the D/E domains and of the A domain with respect to the HAD part. These comparisons suggest that the N-terminal part of the linker helix, which interacts tightly with domains A and E, functions as a hinge region for movement of the A domain with respect to the HAD part.
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Schmitz, Werner
(author)
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Hiltunen, J. Kalervo
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Venkatesan, Rajaram
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Bergmann, Ulrich
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Kiema, Tiila-Riikka
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Wierenga, Rikkert K.
(author)
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Faculty of Biochemistry and Molecular Medicine, University of Oulu, Oulu, Finland;Biocenter Oulu, University of Oulu, Oulu, Finland
(creator_code:org_t)
Related titles
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In:Acta Crystallographica Section D: International Union of Crystallography (IUCr)76:12, s. 1256-12692059-7983
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