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Instruments / Technical Area	Publication Details	Published
I04-Macromolecular Crystallography	FMN-dependent oligomerization of putative lactate oxidase from Pediococcus acidilactici Yashwanth Ashok , Mirko M. Maksimainen , Tuija Kallio , Pekka Kilpeläinen , Lari Lehtiö Plos One 15 DOI: 10.1371/journal.pone.0223870 Diamond Proposal Number(s): [19951] Open Access Show Abstract ▼ Abstract: Lactate oxidases belong to a group of FMN-dependent enzymes and they catalyze a conversion of lactate to pyruvate with a release of hydrogen peroxide. Hydrogen peroxide is also utilized as a read out in biosensors to quantitate lactate levels in biological samples. Aerococcus viridans lactate oxidase is the best characterized lactate oxidase and our knowledge of lactate oxidases relies largely to studies conducted with that particular enzyme. Pediococcus acidilactici lactate oxidase is also commercially available for e.g. lactate measurements, but this enzyme has not been characterized in detail before. Here we report structural characterization of the recombinant enzyme and its co-factor dependent oligomerization. The crystal structures revealed two distinct conformations in the loop closing the active site, consistent with previous biochemical studies implicating the role of loop in catalysis. Despite the structural conservation of active site residues, we were not able to detect either oxidase or monooxygenase activity when L-lactate was used as a substrate. Pediococcus acidilactici lactate oxidase is therefore an example of a misannotation of an FMN-dependent enzyme, which catalyzes likely a so far unknown oxidation reaction.	Feb 2020
I04-1-Macromolecular Crystallography (fixed wavelength)	Multiple crystal forms of human MacroD2 Sarah Wazir , Mirko M. Maksimainen , Lari Lehtiö Acta Crystallographica Section F Structural Biology Communications 76, 477 - 482 DOI: 10.1107/S2053230X20011309 Diamond Proposal Number(s): [19951] Show Abstract ▼ Abstract: MacroD2 is one of the three human macrodomain proteins characterized by their protein-linked mono-ADP-ribosyl-hydrolyzing activity. MacroD2 is a single-domain protein that contains a deep ADP-ribose-binding groove. In this study, new crystallization conditions for MacroD2 were found and three crystal structures of human MacroD2 in the apo state were solved in space groups P41212, P43212 and P43, and refined at 1.75, 1.90 and 1.70 Å resolution, respectively. Structural comparison of the apo crystal structures with the previously reported crystal structure of MacroD2 in complex with ADP-ribose revealed conformational changes in the side chains of Val101, Ile189 and Phe224 induced by the binding of ADP-ribose in the active site. These conformational variations may potentially facilitate design efforts of a MacroD2 inhibitor.	Oct 2020
I03-Macromolecular Crystallography I04-1-Macromolecular Crystallography (fixed wavelength) I04-Macromolecular Crystallography	The peroxisomal zebrafish SCP2-thiolase (type-1) is a weak transient dimer as revealed by crystal structures and native mass spectrometry Tiila-riikka Kiema , Chandan J. Thapa , Mikko Laitaoja , Werner Schmitz , Mirko M. Maksimainen , Toshiyuki Fukao , Juha Rouvinen , Janne Jänis , Rik K. Wierenga Biochemical Journal DOI: 10.1042/BCJ20180788 Open Access Show Abstract ▼ Abstract: The SCP2-thiolase (type-1) functions in the vertebrate peroxisomal, bile acid synthesis pathway, converting 24-keto-THC-CoA and CoA into choloyl-CoA and propionyl-CoA. This conversion concerns the β-oxidation chain shortening of the steroid fatty acyl moiety of 24-keto-THC-CoA. This class of dimeric thiolases has previously been poorly characterized. High resolution crystal structures of the zebrafish SCP2-thiolase (type-1) now reveal an open catalytic site, shaped by residues of both subunits. The structure of its non-dimerised monomeric form has also been captured in the obtained crystals. Four loops at the dimer interface adopt very different conformations in the monomeric form. These loops also shape the active site and their structural changes explain why a competent active site is not present in the monomeric form. Native mass spectrometry studies confirm that the zebrafish SCP2-thiolase (type-1) as well as its human homologue are weak transient dimers in solution. The crystallographic binding studies reveal the mode of binding of CoA and octanoyl-CoA in the active site, highlighting the conserved geometry of the nucleophilic cysteine, the catalytic acid/base cysteine and the two oxyanion holes. The dimer interface of SCP2-thiolase (type-1) is equally extensive as in other thiolase dimers, however it is more polar than any of the corresponding interfaces, which correlates with the notion that the enzyme forms a weak transient dimer. The structure comparison of the monomeric and dimeric forms suggests functional relevance of this property. These comparisons provide also insight into the structural rearrangements that occur when the folded inactive monomers assemble into the mature dimer.	Dec 2018

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