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Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 10/2013, Volume 110, Issue 42, pp. 16808 - 16813
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Organic & Biomolecular Chemistry, ISSN 1477-0520, 01/2019, Volume 17, Issue 17, pp. 4350 - 4358
Pyridoxal 5′-phosphate (PLP) is a versatile cofactor involved in a large variety of enzymatic processes. Most of PLP-catalysed reactions, such as those of... 
Crystal growth | Alanine | Alanine racemase | Deactivation | Deformation mechanisms | Lysine | Inactivation | Buffers | Crystallography | Substrates | Crystal structure
Journal Article
Molecular Microbiology, ISSN 0950-382X, 04/2018, Volume 108, Issue 2, pp. 128 - 142
Journal Article
Scientific Reports, ISSN 2045-2322, 12/2018, Volume 8, Issue 1, pp. 4110 - 8
Lytic transglycosylases (LTs) catalyze the non-hydrolytic cleavage of the bacterial cell wall by an intramolecular transacetalization reaction. This reaction... 
COMPLEX | PEPTIDOGLYCAN | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | SUBSTRATE-ASSISTED CATALYSIS | LYSOZYMES | BETA-HEXOSAMINIDASE | CHITINASE | SIMULATIONS | PARTICIPATION | INSIGHTS | Glutamic acid | Pili | E coli | Cell walls | Secretion | Virulence | Catalysis | Flagella
Journal Article
Journal Article
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, ISSN 1422-0067, 11/2019, Volume 20, Issue 21, p. 5245
Journal Article
EMBO Molecular Medicine, ISSN 1757-4676, 12/2013, Volume 5, Issue 12, pp. 1852 - 1870
The respiratory pathogen Streptococcus pneumoniae has evolved efficient mechanisms to resist oxidative stress conditions and to displace other bacteria in the... 
pneumococci | pneumonia | lipoproteins | oxidative stress | meningitis | Oxidative stress | Meningitis | Lipoproteins | Pneumonia | Pneumococci | MEDICINE, RESEARCH & EXPERIMENTAL | DISULFIDE BOND FORMATION | PROTEIN | BACILLUS-SUBTILIS | METHIONINE SULFOXIDE REDUCTASES | NEISSERIA-MENINGITIDIS | ESCHERICHIA-COLI | N-TERMINAL DOMAIN | PILB | COLONIZATION | HYDROGEN-PEROXIDE PRODUCTION | Virulence | Bacterial Proteins - chemistry | Molecular Sequence Data | Crystallography, X-Ray | Methionine - pharmacology | Recombinant Proteins - biosynthesis | Pneumonia - mortality | Streptococcus pneumoniae - pathogenicity | Methionine - analogs & derivatives | Streptococcus pneumoniae - metabolism | Pneumonia - immunology | Female | Macrophages - immunology | Disease Models, Animal | Macrophages - physiology | Protein Structure, Tertiary | Catalytic Domain | Bacterial Proteins - genetics | Hydrogen Peroxide - pharmacology | Recombinant Proteins - chemistry | Pneumonia - microbiology | Recombinant Proteins - genetics | Animals | Survival Analysis | Bacterial Proteins - metabolism | Mice | Oxidative Stress - drug effects | Phagocytosis | Amino acids | Blood lipids | Thioredoxin | Bacterial pneumonia | Enzymes | Hydrogen peroxide | Pathogenesis | Methionine | Antimicrobial agents | Nasopharynx | Macrophages | Experiments | Streptococcus infections | Antioxidants | Proteins | Bacteria | Oxidation | Reductase | Structure-function relationships
Journal Article
Acta Crystallographica Section A Foundations and Advances, ISSN 2053-2733, 12/2017, Volume 73, Issue a2, pp. C634 - C634
Journal Article
NATURE COMMUNICATIONS, ISSN 2041-1723, 12/2019, Volume 10, Issue 1, pp. 1 - 13
SPOR domains are widely present in bacterial proteins that recognize cell-wall peptidoglycan strands stripped of the peptide stems. This type of peptidoglycan... 
ELUCIDATION | LOCALIZATION | WALL | LYTIC TRANSGLYCOSYLASE | MULTIDISCIPLINARY SCIENCES | VALIDATION | RESISTANCE | SEPARATION | AMIDASES | IDENTIFICATION | PEPTIDOGLYCAN-BINDING
Journal Article
Acta Crystallographica Section D, ISSN 1399-0047, 12/2015, Volume 71, Issue 12, pp. 2526 - 2542
Riboflavin kinases (RFKs) catalyse the phosphorylation of riboflavin to produce FMN. In most bacteria this activity is catalysed by the C‐terminal module of a... 
ATP:riboflavin kinase | FAD synthetase | crystal structure | molecular‐dynamics simulations | conformational changes | substrate binding | Molecular-dynamics simulations | Conformational changes | Crystal structure | Substrate binding | NADPH OXIDASE | MOLECULAR REPLACEMENT | PROTEIN SECONDARY STRUCTURE | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | BIOCHEMICAL RESEARCH METHODS | molecular-dynamics simulations | CRYSTALLOGRAPHY | RIBOFLAVIN KINASE REVEALS | CORYNEBACTERIUM-AMMONIAGENES | KEY RESIDUES | BIOPHYSICS | AMMONIAGENES FAD SYNTHETASE | QUATERNARY ORGANIZATION | CATALYTIC SITE | Nucleotidyltransferases - chemistry | Phosphotransferases (Alcohol Group Acceptor) - chemistry | Protein Multimerization | Bacterial Proteins - chemistry | Molecular Sequence Data | Substrate Specificity | Crystallography, X-Ray | Adenosine Diphosphate - chemistry | Corynebacterium - chemistry | Escherichia coli - metabolism | Nucleotidyltransferases - metabolism | Corynebacterium - enzymology | Recombinant Proteins - metabolism | Promoter Regions, Genetic | Catalytic Domain | Gene Expression | Protein Structure, Secondary | Bacterial Proteins - genetics | Recombinant Proteins - chemistry | Phosphotransferases (Alcohol Group Acceptor) - genetics | Recombinant Proteins - genetics | Flavin Mononucleotide - chemistry | Molecular Dynamics Simulation | Amino Acid Motifs | Phosphotransferases (Alcohol Group Acceptor) - metabolism | Escherichia coli - genetics | Nucleotidyltransferases - genetics | Protein Binding | Bacterial Proteins - metabolism | Ligands | Adenosine Diphosphate - metabolism | Kinetics | Flavin Mononucleotide - metabolism | Structure | Ligases | Phosphotransferases | Crystals | Kinases | Organisms
Journal Article