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Regulation of glutamate metabolism by protein kinases in mycobacteria
It is shown that protein kinase G of Mycobacterium tuberculosis undergoes a pattern of autophosphorylation that is distinct from that of other M.’tuberculosis protein kinases characterized to date and GarA is identified as a substrate for phosphorylation by PknG, which may contribute to the attenuation of virulence.
Conformations of immunoglobulin hypervariable regions
There is a small repertoire of main-chain conformations for at least five of the six hypervariable regions of antibodies, and that the particular conformation adopted is determined by a few key conserved residues.
The crystal structure and mode of action of trans-sialidase, a key enzyme in Trypanosoma cruzi pathogenesis.
Mitochondrial Release of Caspase-2 and -9 during the Apoptotic Process
The data suggest that caspase-2 and -9 zymogens are essentially localized in mitochondria and that the disruption of the outer mitochondrial membrane occurring early during apoptosis may be critical for their subcellular redistribution and activation.
Missense mutations in the catalase‐peroxidase gene, katG, are associated with isoniazid resistance in Mycobacterium tuberculosis
Study of a panel of INH‐resistant clinical isolates using a novel strategy based on the polymerase chain reaction and single‐strand‐conformation polymorphism analysis (PCR‐SSCP) to detect mutations in katG found that in most cases INH resistance was associated with missense mutations while in a small number of strains the gene had been completely, or partially, deleted.
PknB kinase activity is regulated by phosphorylation in two Thr residues and dephosphorylation by PstP, the cognate phospho‐Ser/Thr phosphatase, in Mycobacterium tuberculosis
Results indicate that, as for eukaryotic homologues, phosphorylation of the activation loop provides a regulation mechanism of mycobacterial kinases and strongly suggest that PknB and PstP could work as a functional pair in vivo to control myCobacterial cell growth.
Structural plasticity and catalysis regulation of a thermosensor histidine kinase
- D. Albanesi, Mariana L. Martín, A. Buschiazzo
- BiologyProceedings of the National Academy of Sciences
- 22 September 2009
It is shown that the thermosensitive histidine kinase, DesK, from Bacillus subtilis is cold-activated through specific interhelical rearrangements in its central four-helix bundle domain, suggesting a model in which the transmembrane sensor domain of DesK promotes these structural changes through conformational signals transmitted by the membrane-connecting two-helical coiled-coil.
The Ser/Thr Protein Kinase PknB Is Essential for Sustaining Mycobacterial Growth
It is shown that the pknB gene can be disrupted by allelic replacement in M. tuberculosis and the saprophyte Mycobacterium smegmatis only in the presence of a second functional copy of the gene.
Crystal Structure of the Catalytic Domain of the PknB Serine/Threonine Kinase from Mycobacterium tuberculosis *
- M. Ortiz-Lombardía, F. Pompeo, B. Boitel, P. Alzari
- BiologyThe Journal of Biological Chemistry
- 11 April 2003
The crystal structure of an active form of PknB, one of the four M. tuberculosis kinases that are conserved in the downsized genome of Mycobacterium leprae, is reported, revealing an enzyme in the active state with an unprecedented arrangement of the Gly-rich loop associated with a new conformation of the nucleotide γ-phosphoryl group.
A potent new mode of β-lactamase inhibition revealed by the 1.7 Å X-ray crystallographic structure of the TEM-1–BLIP complex
- N. Strynadka, S. Jensen, P. Alzari, M. James
- Chemistry, BiologyNature Structural Biology
- 1 March 1996
The structure of TEM-1 β-lactamase complexed with the inhibitor BLIP has been determined at 1.7 Å resolution and a β-hairpin loop from domain 1 of BLIP may serve as a template with which to create a new family of peptide-analogue β- lactamases inhibitors.