R. Pérez-Luque

ORCID: 0000-0003-0759-0608
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About
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Research Areas
  • Viral Infections and Immunology Research
  • Animal Disease Management and Epidemiology
  • Viral Infectious Diseases and Gene Expression in Insects
  • Enzyme Structure and Function
  • Bacterial Genetics and Biotechnology
  • Bacteriophages and microbial interactions
  • RNA and protein synthesis mechanisms
  • DNA Repair Mechanisms
  • DNA and Nucleic Acid Chemistry
  • Heme Oxygenase-1 and Carbon Monoxide
  • Neonatal Health and Biochemistry
  • Cancer Research and Treatments
  • Porphyrin Metabolism and Disorders
  • Microbial infections and disease research
  • Vibrio bacteria research studies
  • Aquaculture disease management and microbiota
  • Aldose Reductase and Taurine
  • RNA Research and Splicing
  • Nonlinear Optical Materials Research
  • Vitamin C and Antioxidants Research
  • Animal Virus Infections Studies
  • Protein Interaction Studies and Fluorescence Analysis
  • Biochemical and Molecular Research
  • Protein purification and stability
  • Helicobacter pylori-related gastroenterology studies

Institute for Research in Biomedicine
2008-2023

Institut de Biologia Molecular de Barcelona
2007-2023

Consejo Superior de Investigaciones Científicas
2001-2023

History of Science Society
2011

Universitat de Barcelona
2008

Centro de Investigaciones Biológicas Margarita Salas
2008

Institut de Biomedicina de la Universitat de Barcelona
2008

Centre d’Investigació i Desenvolupament
1998-2005

KU Leuven
2005

University of Bristol
2005

Abstract Double-stranded DNA bacteriophages package their genome at high pressure inside a procapsid through the portal, an oligomeric ring protein located unique capsid vertex. Once has been packaged, tail components assemble on portal to render mature infective virion. The tightly seals ejection conduit until infection, when its interaction with host membrane triggers opening of channel and viral is delivered cell. Using high-resolution cryo-electron microscopy X-ray crystallography, here...

10.1038/s41467-019-11705-9 article EN cc-by Nature Communications 2019-08-20

RNA virus replication is an error-prone event caused by the low fidelity of viral RNA-dependent polymerases. Replication can be decreased further use mutagenic ribonucleoside analogs to a point where genetic information no longer maintained. For foot-and-mouth disease virus, antiviral ribavirin and 5-fluorouracil have been shown mutagenic, contributing extinction through lethal mutagenesis. Here, we report x-ray structure four elongation complexes polymerase 3D obtained in presence natural...

10.1073/pnas.0700518104 article EN Proceedings of the National Academy of Sciences 2007-05-22

Resistance of viruses to mutagenic agents is an important problem for the development lethal mutagenesis as antiviral strategy. Previous studies with RNA have documented that resistance nucleoside analogue ribavirin (1-β-D-ribofuranosyl-1-H-1,2,4-triazole-3-carboxamide) mediated by amino acid substitutions in viral polymerase either increase general template copying fidelity enzyme or decrease incorporation into RNA. Here we describe experiments show replication picornavirus pathogen...

10.1371/journal.ppat.1001072 article EN cc-by PLoS Pathogens 2010-08-26

Abstract Mycoplasma pneumoniae is a bacterial human pathogen that causes primary atypical pneumonia. M. motility and infectivity are mediated by the immunodominant proteins P1 P40/P90, which form transmembrane adhesion complex. Here we report structure of P1, determined X-ray crystallography cryo-electron microscopy, P40/P90. Contrary to what had been suggested, binding site for sialic acid was found in P40/P90 not P1. Genetic clinical variability concentrates on N-terminal domain surfaces...

10.1038/s41467-020-18777-y article EN cc-by Nature Communications 2020-10-14

ABSTRACT The FucO protein, a member of the group III “iron-activated” dehydrogenases, catalyzes interconversion between l -lactaldehyde and -1,2-propanediol in Escherichia coli . three-dimensional structure complex with NAD + was solved, presence iron crystals confirmed by X-ray fluorescence. presented here is first for bacterial dehydrogenases shown experimentally to contain iron. forms dimer, which each monomer folds into an α/β dinucleotide-binding N-terminal domain all-α-helix C-terminal...

10.1128/jb.187.14.4957-4966.2005 article EN Journal of Bacteriology 2005-07-01

Helicobacter pylori produces one monofunctional catalase, encoded by katA (hp0875). The crystal structure of H. catalase (HPC) has been determined and refined at 1.6 Å with crystallographic agreement factors R Rfree 17.4 21.9%, respectively. exhibits P21212 space group symmetry contains two protein subunits in the asymmetric unit. core HPC subunit, including disposition a heme b prosthetic group, is closely related to those other catalases, although it appears be only clade III that...

10.1021/bi035663i article EN Biochemistry 2004-02-27

ABSTRACT Passage of poliovirus (PV) or foot-and-mouth disease virus (FMDV) in the presence ribavirin (R) selected for viruses with decreased sensitivity to R, which included different mutations their polymerase (3D): G64S located finger subdomain case PV and M296I within loop β9-α11 at active site FMDV. To investigate why disparate substitutions were two closely related 3Ds, we constructed FMDVs a 3D that either G62S (the equivalent replacement FMDV G64S), M296I, both substitutions. G62S,...

10.1128/jvi.02420-09 article EN Journal of Virology 2010-04-15

Significance Nearly 90% of lethal antibiotic-resistant infections in the United States are caused by Gram-positive pathogens, with Staphylococcus aureus accounting for more than one-half these. Antibiotic resistance is often encoded plasmids and integrative elements that exchanged between bacteria through conjugative DNA transfer. During conjugation, a relaxase protein binds, nicks, covalently attaches to 5′-end DNA, guiding it recipient cell, where restores its circular closed form. We show...

10.1073/pnas.1702971114 article EN Proceedings of the National Academy of Sciences 2017-07-24

UlaR is a DNA binding protein of the DeoR family eubacterial transcriptional repressors which maintains utilization l-ascorbate ula regulon in repressed state. The availability growth medium releases UlaR-mediated repression on regulon, thereby activating transcription. molecular details this induction by have remained elusive to date. Here we identified 6-phosphate as direct effector UlaR; using combination site-directed mutagenesis, gel retardation, isothermal titration calorimetry, and...

10.1021/bi800748x article EN Biochemistry 2008-10-10

Of the nine genes comprising L-rhamnose operon of Rhizobium leguminosarum, rhaU has not been assigned a function. The construction Delta strain revealed growth phenotype that was slower than wild-type strain, although ultimate cell yields were equivalent. transport into and rate its phosphorylation unaffected by mutation. RhaU exhibits weak sequence similarity to formerly hypothetical protein YiiL Escherichia coli recently characterized as an mutarotase. To characterize further, His-tagged...

10.1128/jb.01120-07 article EN Journal of Bacteriology 2007-12-22

ToxR, a Vibrio cholerae transmembrane one-component signal transduction factor, lies within regulatory cascade that results in the expression of ToxT, toxin coregulated pilus, and cholera toxin. While ToxR has been extensively studied for its ability to activate or repress various genes V. , here we present crystal structures cytoplasmic domain bound DNA at toxT ompU promoters. The confirm some predicted interactions, yet reveal other unexpected promoter interactions with implications...

10.1073/pnas.2304378120 article EN cc-by-nc-nd Proceedings of the National Academy of Sciences 2023-07-10

Decarboxylation of malonyl-CoA to acetyl-CoA by decarboxylase (MCD; EC 4.1.1.9) is an essential facet in the regulation fatty acid metabolism. The structure human peroxisomal MCD reveals a molecular tetramer that best described as dimer structural heterodimers, which two subunits present markedly different conformations. This organization consistent with half-of-the-sites reactivity. Each subunit has all-helix N-terminal domain and catalytic C-terminal acetyltransferase fold (GNAT...

10.1074/jbc.m112.443846 article EN cc-by Journal of Biological Chemistry 2013-03-13

A limited repertoire of PPP family serine/threonine phosphatases with a highly conserved catalytic domain acts on thousands protein targets to orchestrate myriad central biological roles. major structural reorganization human calcineurin, ubiquitous Ser/Thr regulated by calcium and calmodulin targeted immunosuppressant drugs cyclosporin FK506, is unveiled here. The new conformation involves trans- cis- isomerization proline in the SAPNY sequence, across PPPs, remodels main regulatory site...

10.1371/journal.pone.0134569 article EN cc-by PLoS ONE 2015-08-06

The large subunit catalase HPII from Escherichia coli can be truncated by proteolysis to a structure similar small catalases. Mass spectrometry analysis indicates that there is some heterogeneity in the precise cleavage sites, but approximately 74 N-terminal residues, 189 C-terminal and 9−11-residue internal fragment, including residues 298−308, are removed. Crystal refinement at 2.8 Å reveals tertiary quaternary of native enzyme retained with only very subtle changes despite loss 36%...

10.1021/bi047277m article EN Biochemistry 2005-03-25

ABSTRACT A crucial element in the horizontal transfer of mobilizable and conjugative plasmids is relaxase, a single-stranded endonuclease that nicks origin ( oriT ) plasmid DNA. The relaxase pMV158 MobM (494 residues). In solution, forms dimer through its C-terminal domain, which proposed to anchor protein cell membrane participate type 4 secretion system (T4SS) protein-protein interactions. order gain deeper insight into structural requirements for efficient DNA catalysis, we studied two...

10.1128/jb.02264-12 article EN Journal of Bacteriology 2013-04-27

Medium-resolution cryo-electron microscopy maps, in particular when they include a significant number of α-helices, may allow the building partial models that are useful for molecular-replacement searches large crystallographic structures homologs not available and experimental phasing has failed. Here, as an example, solution structure bacteriophage portal using 30% model built into 7.8 Å resolution cryo-EM map is shown. Inspection self-rotation function allowed correct oligomerization...

10.1107/s2059798320015156 article EN cc-by Acta Crystallographica Section D Structural Biology 2020-12-17
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