Montse Tersa

Discovery of Stereoselective Targeted Covalent Inhibitors of the RAB27-Effector Protein–Protein Interaction

Elena De Vita, Adam M. Thomas, Delia Brustur, Montse Tersa et autres

Abstract RAB27A and RAB27B are homologous small GTPases that regulate intracellular vesicle trafficking, orchestrating endocytic and exocytic processes that affect cellular communication, immune responses, and the dynamics of the cellular microenvironment. Through their interactions with effector proteins, RAB27A/B plays roles in tumor …

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Discovery of stereoselective targeted covalent inhibitors of the RAB27-effector protein-protein interaction

Elena De Vita, Adam Thomas, Delia Brustur, Montse Tersa et autres

Abstract RAB27A and RAB27B are homologous small GTPases that regulate intracellular vesicle trafficking, orchestrating endocytic and exocytic processes that affect cellular communication, immune responses, and dynamics of the cellular microenvironment. Through their interactions with effector proteins, RAB27A/B play roles in tumor metastasis …

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Identification of the first structurally validated covalent ligands of the small GTPase RAB27A

Mostafa Jamshidiha, Thomas Lanyon‐Hogg, Charlotte L. Sutherell, Gregory B. Craven et autres

a conserved tryptophan-phenylalanine (WF) dipeptide motif. To obtain structural insight into the ligandability of this pocket, a novel construct was designed fusing Rab27A to part of an effector protein (fRab27A), allowing crystallisation of Rab27A in high throughput. The paradigm of KRas covalent …

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Molecular ruler mechanism and interfacial catalysis of the integral membrane acyltransferase PatA

Itxaso Anso, Luis G.M. Basso, Lei Wang, Alberto Marina et autres

. We demonstrate by electron spin resonance spectroscopy and surface plasmon resonance that PatA is an integral membrane acyltransferase tightly anchored to anionic lipid bilayers, using a two-helix structural motif and electrostatic interactions. PatA dictates the acyl chain composition of the glycolipid …

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Dissecting the Structural and Chemical Determinants of the “Open-to-Closed” Motion in the Mannosyltransferase PimA from Mycobacteria

Ane Rodrigo‐Unzueta, Mattia Ghirardello, S. Urresti, Ignacio Delso et autres

. PimA undergoes functionally important conformational changes, including (i) α-helix-to-β-strand and β-strand-to-α-helix transitions and (ii) an "open-to-closed" motion between the two Rossmann-fold domains, a conformational change that is necessary to generate a catalytically competent active site. In previous work, we established that …

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Unveiling the activation dynamics of a fold-switch bacterial glycosyltransferase by 19F NMR

Jobst Liebau, Montse Tersa, Beatriz Trastoy, Joan Patrick et autres

Fold-switch pathways remodel the secondary structure topology of proteins in response to the cellular environment. It is a major challenge to understand the dynamics of these folding processes. Here, we conducted an in-depth analysis of the α-helix–to–β-strand and β-strand–to–α-helix transitions and domain …

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The Molecular Mechanism of Substrate Recognition and Catalysis of the Membrane Acyltransferase PatA from Mycobacteria

Montse Tersa, Lluı́s Raich, Beatriz Trastoy, Jacques Prandi et autres

Glycolipids play a central role in a variety of important biological processes in all living organisms. PatA is a membrane acyltransferase involved in the biosynthesis of phosphatidyl- myo -inositol mannosides (PIMs), key structural elements, and virulence factors of Mycobacterium tuberculosis . PatA …

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Structural basis for selective recognition of acyl chains by the membrane-associated acyltransferase PatA

David Albesa-Jové, Zuzana Svetlíková, Montse Tersa, Enea Sancho‐Vaello et autres

The biosynthesis of phospholipids and glycolipids are critical pathways for virtually all cell membranes. PatA is an essential membrane associated acyltransferase involved in the biosynthesis of mycobacterial phosphatidyl-myo-inositol mannosides (PIMs). The enzyme transfers a palmitoyl moiety from palmitoyl-CoA to the 6-position of …

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Crystal structure of membrane associated PatA from Mycobacterium smegmatis in complex with palmitate - C 2 space group

Zuzana Svetlíková, Ana Carreras‐González, Montse Tersa, Enea Sancho‐Vaello et autres

Crystal structure of membrane associated PatA from Mycobacterium smegmatis in complex with S-hexadecyl Coenzyme A - P21 space group

Zuzana Svetlíková, Ana Carreras‐González, Montse Tersa, Enea Sancho‐Vaello et autres

The Redox State Regulates the Conformation of Rv2466c to Activate the Antitubercular Prodrug TP053

Natalia Comino, Montse Tersa, Elisabeth Mohorko, S. Urresti et autres

Rv2466c is a key oxidoreductase that mediates the reductive activation of TP053, a thienopyrimidine derivative that kills replicating and non-replicating Mycobacterium tuberculosis, but whose mode of action remains enigmatic. Rv2466c is a homodimer in which each subunit displays a modular architecture comprising …

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Crystal structure of Rv2466c and oxidoreductase from Mycobacterium tuberculosis in its reduced state

S. Urresti, Natalia Comino, Montse Tersa, Marcelo E. Guerin