Antonio Romero

Centro de Investigaciones Biológicas Margarita Salas

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Co-Authors

Francisco J. Medrano

Centro de Investigaciones Biológicas Margarita Salas

Hans‐Joachim Gabius

Ludwig-Maximilians-Universität München

Federico M. Ruiz

Centro de Investigaciones Biológicas Margarita Salas

Juan J. Calvete

Instituto de Biomedicina de Valencia

ÁT

Ángel T. Martı́nez

Centro de Investigaciones Biológicas Margarita Salas

Dolores Solı́s

Consejo Superior de Investigaciones Científicas

Herbert Kaltner

Ludwig-Maximilians-Universität München

Francisco J. Ruiz‐Dueñas

Centro de Investigaciones Biológicas Margarita Salas

ΑV

Α. Vegas

Universidad de Burgos

Líbia Sanz

Instituto de Biomedicina de Valencia

Cooperative Institutions

European Organization for Nuclear Research

209

Centre National de la Recherche Scientifique

208

Iowa State University

162

Consejo Superior de Investigaciones Científicas

156

Institute of High Energy Physics

100

A. Alikhanyan National Laboratory

Institut National de Physique Nucléaire et de Physique des Particules

Centro de Investigaciones Biológicas Margarita Salas

University of Adelaide

Karlsruhe Institute of Technology

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Purification, crystallization and identification by X-ray analysis of a prostate kallikrein from horse seminal plasma

Acta Crystallographica Section D Biological Crystallography (2001)

Ana Luı́sa Carvalho João M.L. Dias Líbia Sanz Antonio Romero Juan J. Calvete

The purification, crystallization and identification by X-ray diffraction analysis of a horse kallikrein is reported. The protein was purified from horse seminal plasma. Crystals belong to space group C2 and the structure was solved by the MIRAS method, with two heavy-atom derivatives of mercury and platinum. X-ray diffraction data to 1.42 Å resolution were collected at the ESRF synchrotron-radiation source.

Protein crystallization

10.1107/s0907444901009805

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Citations (3)

The crystal structure of nickel(I1)-azurin

José M. Moratal Antonio Romero Aurea Perales-Alarcon Hermás R. Jiménez

Azurin

Source

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Citations (1)

The structure of VgrG1, the needle tip of the bacterial Type VI Secretion System

Mercedes Spínola‐Amilibia Irene Davó-Siguero Flávia Montanari Ruiz Elena Santillana Francisco J. Medrano

10.2210/pdb4uhv/pdb

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Citations (0)

CRYSTAL STRUCTURE OF FUNGAL VERSATILE PEROXIDASE FROM PLEUROTUS ERYNGII SEPTUPLE MUTANT E37K, H39R, V160A, T184M, Q202L, D213A & G330R

Francisco J. Medrano Antonio Romero

Pleurotus eryngii

Pleurotus

10.2210/pdb5fnb/pdb

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Citations (0)

Members of the Galectin Network with Deviations from the Canonical Sequence Signature. 2. Galectin-Related Protein (GRP)

Trends in Glycoscience and Glycotechnology (2018)

Joachim C. Manning Gabriel García Caballero Federico M. Ruiz Antonio Romero Herbert Kaltner

Galectin-related protein (GRP) is present in vertebrates. Sequence comparisons between GRPs from diverse species reveal an unusually high degree of similarity indicative of a strong positive selection. In solution, human and chicken GRPs are monomers irrespective of the presence of the 36-amino-acid-long extension of the core structure at the N-terminus. They are devoid of ability to bind lactose due to severe deviations from the respective sequence signature. Crystallography disclosed distortion of the binding-site architecture that precludes accommodation of lactose. The recent characterization of expression of chicken GRP (C-GRP) enables complete galectin network analysis in this organism. When tested in a panel of developing and adult organs, C-GRP presence was detected in bursa of Fabricius. Its epithelium and vessels as well as bursal B cells are positive in immunohistochemistry. In the B lymphocytes, C-GRP was predominantly cytoplasmic, whereas the chicken tandem-repeat-type galectin, the second member of the galectin family expressed in these cells, was detected at the surface. Binding of labeled C-GRP to cells and sections was blocked by heparin. These data illustrate disparities in expression and ligand profiles within the galectin family and hereby stimulate interest to perform respective mapping for mammalian GRPs as step to define its physiological function(s).

Galectin

Bursa of Fabricius

Sequence (biology)

10.4052/tigg.1727.1se

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Citations (13)

Design, Synthesis, and Crystal Structures of 6-Alkylidene-2′-Substituted Penicillanic Acid Sulfones as Potent Inhibitors of Acinetobacter baumannii OXA-24 Carbapenemase

Journal of the American Chemical Society (2010)

Germán Bou Elena Santillana Anjaneyulu Sheri Alejandro Beceiro Jared M. Sampson

Class D β-lactamases represent a growing and diverse class of penicillin-inactivating enzymes that are usually resistant to commercial β-lactamase inhibitors. As many such enzymes are found in multi-drug resistant (MDR) Acinetobacter baumannii and Pseudomonas aeruginosa, novel β-lactamase inhibitors are urgently needed. Five unique 6-alkylidene-2′-substituted penicillanic acid sulfones (1−5) were synthesized and tested against OXA-24, a clinically important β-lactamase that inactivates carbapenems and is found in A. baumannii. Based upon the roles Tyr112 and Met223 play in the OXA-24 β-lactamase, we also engineered two variants (Tyr112Ala and Tyr112Ala,Met223Ala) to test the hypothesis that the hydrophobic tunnel formed by these residues influences inhibitor recognition. IC50 values against OXA-24 and two OXA-24 β-lactamase variants ranged from 10 ± 1 (4 vs WT) to 338 ± 20 nM (5 vs Tyr112Ala, Met223Ala). Compound 4 possessed the lowest Ki (500 ± 80 nM vs WT), and 1 possessed the highest inactivation efficiency (kinact/Ki = 0.21 ± 0.02 μM−1 s−1). Electrospray ionization mass spectrometry revealed a single covalent adduct, suggesting the formation of an acyl-enzyme intermediate. X-ray structures of OXA-24 complexed to four inhibitors (2.0−2.6 Å) reveal the formation of stable bicyclic aromatic intermediates with their carbonyl oxygen in the oxyanion hole. These data provide the first structural evidence that 6-alkylidene-2′-substituted penicillin sulfones are effective mechanism-based inactivators of class D β-lactamases. Their unique chemistry makes them developmental candidates. Mechanisms for class D hydrolysis and inhibition are discussed, and a pathway for the evolution of the BlaR1 sensor of Staphylococcus aureus to the class D β-lactamases is proposed.

Acinetobacter baumannii

10.1021/ja104092z

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Citations (67)

A new type of Class C β-lactamases defined by PIB-1. A metal-dependent carbapenem-hydrolyzing β-lactamase, from Pseudomonas aeruginosa: Structural and functional analysis

International Journal of Biological Macromolecules (2024)

Francisco J. Medrano Sara Hernando‐Amado José Luis Martínez Antonio Romero

Carbapenem

Hydrolase

10.1016/j.ijbiomac.2024.134298

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Citations (1)