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Instruments / Technical Area	Publication Details	Published
	Membrane's Eleven: heavy-atom derivatives of membrane-protein crystals Preben Morth , Thomas Lykke-Møller Sorensen , Poul Nissen Acta Crystallographica Section D Biological Crystallography 62 (8), 877 - 882 DOI: 10.1107/S0907444906023547 PMID: 16855303 Show Abstract ▼ Abstract: A database has been assembled of heavy-atom derivatives used in the structure determination of membrane proteins. The database can serve as a guide to the design of experiments in the search for heavy-atom derivatives of new membrane-protein crystals. The database pinpoints organomercurials, platinum(II) and trimethyllead compounds as being particularly useful. On the other hand, lanthanide and uranyl compounds are poorly represented, which may be a consequence of these compounds having aggressive effects in crystal-soaking procedures. Furthermore, the database highlights the variety of methods applied in the preparation of heavy-atom-derivatized crystals and in phasing. Cocrystallization can be further exploited. Phases have predominantly been obtained by SIRAS/MIRAS methods rather than SAD/MAD in recent structure determinations.	Aug 2006
I02-Macromolecular Crystallography	Crystal structure of a two-domain fragment of hepatocyte growth factor activator inhibitor-1 Zebin Hong , Laura De Meulemeester , Annemarie Jacobi , Jan Skov Pedersen , J. Preben Morth , Peter A. Andreasen , Jan K. Jensen Journal Of Biological Chemistry 291, 14340 - 14355 DOI: 10.1074/jbc.M115.707240 Diamond Proposal Number(s): [9107] Open Access Show Abstract ▼ Abstract: Hepatocyte growth factor activator inhibitor-1 (HAI-1) is a type I transmembrane protein and inhibitor of several serine proteases, including hepatocyte growth factor activator and matriptase. The protein is essential for development as knock-out mice die in utero due to placental defects caused by misregulated extracellular proteolysis. HAI-1 contains two Kunitz-type inhibitor domains (Kunitz), which are generally thought of as a functionally self-contained protease inhibitor unit. This is not the case for HAI-1, where our results reveal how interdomain interactions have evolved to stimulate the inhibitory activity of an integrated Kunitz. Here we present an x-ray crystal structure of an HAI-1 fragment covering the internal domain and Kunitz-1. The structure reveals not only that the previously uncharacterized internal domain is a member of the polycystic kidney disease domain family but also how the two domains engage in interdomain interactions. Supported by solution small angle x-ray scattering and a combination of site-directed mutagenesis and functional assays, we show that interdomain interactions not only stabilize the fold of the internal domain but also stimulate the inhibitory activity of Kunitz-1. By completing our structural characterization of the previously unknown N-terminal region of HAI-1, we provide new insight into the interplay between tertiary structure and the inhibitory activity of a multidomain protease inhibitor. We propose a previously unseen mechanism by which the association of an auxiliary domain stimulates the inhibitory activity of a Kunitz-type inhibitor (i.e. the first structure of an intramolecular interaction between a Kunitz and another domain).	Jul 2016
I02-Macromolecular Crystallography	A fundamental catalytic difference between zinc and manganese dependent enzymes revealed in a bacterial isatin hydrolase Theis Sommer , Kaare Bjerregaard-Andersen , Lalita Uribe , Michael Etzerodt , Gregor Diezemann , Jürgen Gauss , Michele Cascella , J. Preben Morth Scientific Reports 8 DOI: 10.1038/s41598-018-31259-y Diamond Proposal Number(s): [9107] Open Access Show Abstract ▼ Abstract: The catalytic mechanism of the cyclic amidohydrolase isatin hydrolase depends on a catalytically active manganese in the substrate-binding pocket. The Mn2+ ion is bound by a motif also present in other metal dependent hydrolases like the bacterial kynurenine formamidase. The crystal structures of the isatin hydrolases from Labrenzia aggregata and Ralstonia solanacearum combined with activity assays allow for the identification of key determinants specific for the reaction mechanism. Active site residues central to the hydrolytic mechanism include a novel catalytic triad Asp-His-His supported by structural comparison and hybrid quantum mechanics/classical mechanics simulations. A hydrolytic mechanism for a Mn2+ dependent amidohydrolases that disfavour Zn2+ as the primary catalytically active site metal proposed here is supported by these likely cases of convergent evolution. The work illustrates a fundamental difference in the substrate-binding mode between Mn2+ dependent isatin hydrolase like enzymes in comparison with the vast number of Zn2+ dependent enzymes.	Aug 2018

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