Iván Angulo
Spanish National Research Council
10 Papers
55 Citations
Iván Angulo is an academic researcher from Spanish National Research Council. The author has contributed to research in topics: Lactobacillus hilgardii & Ornithine transcarbamylase. The author has an hindex of 5, co-authored 10 publications.
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Papers
The structure of the C-terminal domain of the protein kinase AtSOS2 bound to the calcium sensor AtSOS3
María José Sánchez-Barrena,Hiroaki Fujii,Iván Angulo,Martín Martínez-Ripoll,Jian-Kang Zhu,Armando Albert +5 more
TL;DR: The crystal structure of the binary complex of Ca-SOS3 with the C-terminal regulatory moiety of SOS2 resolves central questions regarding the dual function of SOS1 as a kinase and a phosphatase-binding protein and reveals the basis of the molecular function of this family of kinases.
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p-Coumaric acid decarboxylase from Lactobacillus plantarum: Structural insights into the active site and decarboxylation catalytic mechanism
Héctor Rodríguez,Iván Angulo,Blanca de las Rivas,Nuria E. Campillo,Juan A. Páez,Rosario Muñoz,José M. Mancheño +6 more
TL;DR: Insight is reported into the structural basis of catalysis for the homodimeric PDC from Lactobacillus plantarum and a two‐step catalytic mechanism for decarboxylation of p‐coumaric acid by PDCs where Glu71 is involved in proton transfer and Tyr18 and Tyr20 are involved in the proper substrate orientation and in the release of the CO2 product.
High-resolution structural insights on the sugar-recognition and fusion tag properties of a versatile β-trefoil lectin domain from the mushroom Laetiporus sulphureus.
Iván Angulo,Iván Acebrón,Blanca de las Rivas,Rosario Muñoz,Ignacio Rodríguez-Crespo,Margarita Menéndez,Pedro García,Hiroaki Tateno,Irwin J. Goldstein,Begoña Pérez-Agote,José M. Mancheño +10 more
TL;DR: This work analyzed at high resolution the sugar-binding mode of the recombinant N-terminal ricin-B domain of the hemolytic protein LSLa from the mushroom Laetiporus sulphureus and provides functional in vitro evidence suggesting that, together with its putative receptor-binding role, this module may also increase the solubility of its membrane pore-forming partner.
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Crystal structure of the hexameric catabolic ornithine transcarbamylase from Lactobacillus hilgardii: Structural insights into the oligomeric assembly and metal binding.
Blanca de las Rivas,Gavin C. Fox,Iván Angulo,Martin Martinez Ripoll,Héctor Rodríguez,Rosario Muñoz,José M. Mancheño +6 more
TL;DR: The crystal structure of cOTC from the lactic acid bacteria Lactobacillus hilgardii is refined to 2.1 A resolution and reveals that Lh-cOTC forms a hexameric assembly, which represents a new oligomeric state within the members of the ornithine transcarbamylase family that are typically homotrimeric or homododecameric.
18
Crystallization and preliminary crystallographic analysis of the catalytic module of endolysin from Cp-7, a phage infecting Streptococcus pneumoniae
TL;DR: As part of the life cycle of the pneumococcal phage Cp-7, the endolysin Cpl-7 cleaves the glycosidic beta1,4 bonds between N-acetylmuramic acid and N- acetylglucosamine in the pneumitiscal cell wall, resulting in bacterial lysis.