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of 14
pro vyhledávání: '"Preethi Ragunathan"'
Autor:
Preethi Ragunathan, Divya Sridaran, Anja Weigel, Sarah Shabayek, Barbara Spellerberg, Karthe Ponnuraj
Publikováno v:
PLoS ONE, Vol 8, Iss 6, p e67517 (2013)
Lmb is a 34 kDa laminin binding surface adhesin of Streptococcus agalactiae. The structure of Lmb reported by us recently has shown that it consists of a metal binding crevice, in which a zinc ion is coordinated to three highly conserved histidines.
Externí odkaz:
https://doaj.org/article/8768567b659342ee82212129f28b1d21
Publikováno v:
ACS Omega. 8:7989-8000
Autor:
Upasana Sridharan, Thirumananseri Kumarevel, Karthe Ponnuraj, Shigeyuki Yokoyama, Preethi Ragunathan, Seiki Kuramitsu
Publikováno v:
Biochemical and Biophysical Research Communications. 547:96-101
Carbonic anhydrases (CA) are the most ubiquitous ancient zinc metalloenzymes known. Here we report the structural and functional analysis of a hypothetical protein GK2848 from Geobacillus kaustophilus. The analysis revealed that it belongs to the γ-
Publikováno v:
Journal of Biomolecular Structure and Dynamics. 40:6272-6285
Alternate sigma factors play a major role in the survival of pathogenic bacteria such as Streptococcus pyogenes in adverse environment conditions. Stress induced sigma factors mediate gene expression under conditions of pathogenesis, dormancy and unu
Publikováno v:
Journal of Biomolecular Structure and Dynamics. 37:714-725
Metal-binding receptors are one of the extracellular components of ATP-binding cassette transporters that are essential for regulation of metal homeostasis in bacteria. Laminin-binding adhesin (Lmb) of Streptococcus agalactiae falls under this class
Publikováno v:
RSC Advances. 6:91824-91835
Pneumococcal adherence and virulence factor A (PavA) were first identified in Streptococcus pneumoniae as an adhesin binding to fibronectin and studies suggested that it is an important virulence determinant. Homologs of PavA are found in many Gram-p
Autor:
Preethi Ragunathan, Karthe Ponnuraj
Publikováno v:
The Protein Journal. 30:159-166
Streptococcus agalactiae is a leading cause of bacterial sepsis and meningitis in neonates. FbsA, a fibrinogen receptor of S. agalactiae is highly repetitive protein with each repeat containing 16 amino acids. The protein sequence of FbsA shows no ho
Publikováno v:
Journal of Biomolecular Structure and Dynamics. 25:183-188
Leptin, the ob gene product, is a 167 amino acid polypeptide known to play a key role in regulating the fat stores of the body and is found in all eukaryotes, including mammals, aves, and also in invertebrates. To gain insight into the structure-func
Publikováno v:
Acta Crystallographica Section F Structural Biology and Crystallization Communications. 65:492-494
Laminin-binding protein (Lmb), a surface-exposed lipoprotein from Streptococcus agalactiae (group B streptococcus), mediates attachment to human laminin and plays a crucial role in the adhesion/invasion of eukaryotic host cells. However, the structur
Autor:
Karthe Ponnuraj, Preethi Ragunathan, Gokul Raghunath, Thirumananseri Kumarevel, Shigeyuki Yokoyama, Seiki Kuramitsu
Publikováno v:
Acta crystallographica. Section F, Structural biology and crystallization communications. 69(Pt 2)
GK2848, a hypothetical protein from the thermophilic organism Geobacillus kaustophilus, was cloned and overexpressed in Escherichia coli. The protein was purified to homogeneity using Ni-NTA affinity-column and gel-filtration chromatography. The puri