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Instruments / Technical Area	Publication Details	Published	Actions
I23-Long wavelength MX	Experimental phasing with vanadium and application to nucleotide-binding membrane proteins Kamel El Omari , Nada Mohamad , Kiran Bountra , Ramona Duman , Maria Romano , Katja Schlegel , Hok-sau Kwong , Vitaliy Mykhaylyk , Claus Olesen , Jesper Vuust Moller , Maike Bublitz , Konstantinos Beis , Armin Wagner Iucrj 7 DOI: 10.1107/S2052252520012312 Open Access Show Abstract ▼ Abstract: The structure determination of soluble and membrane proteins can be hindered by the crystallographic phase problem, especially in the absence of a suitable homologous structure. Experimental phasing is the method of choice for novel structures; however, it often requires heavy-atom derivatization, which can be difficult and time-consuming. Here, a novel and rapid method to obtain experimental phases for protein structure determination by vanadium phasing is reported. Vanadate is a transition-state mimic of phosphoryl-transfer reactions and it has the advantage of binding specifically to the active site of numerous enzymes catalyzing this reaction. The applicability of vanadium phasing has been validated by determining the structures of three different protein–vanadium complexes, two of which are integral membrane proteins: the rabbit sarcoplasmic reticulum Ca2+-ATPase, the antibacterial peptide ATP-binding cassette transporter McjD from Escherichia coli and the soluble enzyme RNAse A from Bos taurus. Vanadium phasing was successful even at low resolution and despite severe anisotropy in the data. This method is principally applicable to a large number of proteins, representing six of the seven Enzyme Commission classes. It relies exclusively on the specific chemistry of the protein and it does not require any modifications, making it a very powerful addition to the phasing toolkit. In addition to the phasing power of this technique, the protein–vanadium complexes also provide detailed insights into the reaction mechanisms of the studied proteins.	Nov 2020
I04-Macromolecular Crystallography	Mip6 binds directly to the Mex67 UBA domain to maintain low levels of Msn2/4 stress‐dependent mRNAs Manuel Martín‐expósito , Maria‐eugenia Gas , Nada Mohamad , Carme Nuño‐cabanes , Ana Tejada‐colón , Pau Pascual‐garcía , Lorena De La Fuente , Belén Chaves‐arquero , Jonathan Merran , Jeffry Corden , Ana Conesa , José Manuel Pérez‐cañadillas , Jeronimo Bravo , Susana Rodríguez‐navarro Embo Reports 20 DOI: 10.15252/embr.201947964 Diamond Proposal Number(s): [10121] Show Abstract ▼ Abstract: RNA‐binding proteins (RBPs) participate in all steps of gene expression, underscoring their potential as regulators of RNA homeostasis. We structurally and functionally characterize Mip6, a four‐RNA recognition motif (RRM)‐containing RBP, as a functional and physical interactor of the export factor Mex67. Mip6‐RRM4 directly interacts with the ubiquitin‐associated (UBA) domain of Mex67 through a loop containing tryptophan 442. Mip6 shuttles between the nucleus and the cytoplasm in a Mex67‐dependent manner and concentrates in cytoplasmic foci under stress. Photoactivatable ribonucleoside‐enhanced crosslinking and immunoprecipitation experiments show preferential binding of Mip6 to mRNAs regulated by the stress‐response Msn2/4 transcription factors. Consistent with this binding, MIP6 deletion affects their export and expression levels. Additionally, Mip6 interacts physically and/or functionally with proteins with a role in mRNA metabolism and transcription such as Rrp6, Xrn1, Sgf73, and Rpb1. These results reveal a novel role for Mip6 in the homeostasis of Msn2/4‐dependent transcripts through its direct interaction with the Mex67 UBA domain.	Oct 2019

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