scholarly journals Conformational studies of the C-terminal 16-amino-acid-residue fragment of the B3 domain of the immunoglobulin binding protein G fromStreptococcus

Biopolymers ◽  
2009 ◽  
Vol 91 (1) ◽  
pp. 37-51 ◽  
Author(s):  
Agnieszka Skwierawska ◽  
Stanisław Ołdziej ◽  
Adam Liwo ◽  
Harold A. Scheraga
Keyword(s):  
Amino Acid ◽  
Amino Acid Residue ◽  
Binding Protein ◽  
Protein G ◽  
Conformational Studies ◽  
Immunoglobulin Binding Protein ◽  
B3 Domain ◽  
Immunoglobulin Binding

scholarly journals Conformational studies of the α-helical 28-43 fragment of the B3 domain of the immunoglobulin binding protein G fromStreptococcus

Biopolymers ◽  
2008 ◽  
Vol 89 (11) ◽  
pp. 1032-1044 ◽  
Author(s):  
Agnieszka Skwierawska ◽  
Sylwia Rodziewicz-Motowidło ◽  
Stanisław Ołdziej ◽  
Adam Liwo ◽  
Harold A. Scheraga
Keyword(s):  
Binding Protein ◽  
Protein G ◽  
Conformational Studies ◽  
Immunoglobulin Binding Protein ◽  
B3 Domain ◽  
Immunoglobulin Binding

scholarly journals Amino acid sequence of the penicillin-binding protein/dd-peptidase of Streptomyces K15. Predicted secondary structures of the low Mr penicillin-binding proteins of class A

1991 ◽  
Vol 279 (1) ◽  
pp. 223-230 ◽  
Author(s):  
P Palomeque-Messia ◽  
S Englebert ◽  
M Leyh-Bouille ◽  
M Nguyen-Distèche ◽  
C Duez ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Residue ◽  
Active Sites ◽  
Binding Protein ◽  
Secondary Structures ◽  
Peptide Sequence ◽  
Penicillin Binding Protein ◽  
Signal Peptide Sequence ◽  
Beta Lactamases ◽  
Class A

The low-Mr penicillin-binding protein (PBP)/DD-transpeptidase of Streptomyces K15 is synthesized in the form of a 291-amino acid-residue precursor possessing a cleavable 29-amino acid-residue signal peptide. Sequence-similarity searches and hydrophobic-cluster analysis show that the Streptomyces K15 enzyme, the Escherichia coli PBPs/DD-carboxy-peptidases 5 and 6, the Bacillus subtilis PBP/DD-carboxypeptidase 5 and the spoIIA product (a putative PBP involved in the sporulation of B. subtilis) are structurally related and form a distinct class A of low-Mr PBPs/DD-peptidases. The distribution of the hydrophobic clusters along the amino acid sequences also shows that the Streptomyces K15 PBP, and by extension the other PBPs of class A, have similarity in the polypeptide folding, with the beta-lactamases of class A, with as reference the Streptomyces albus G and Staphylococcus aureus beta-lactamases of known three-dimensional structure. This comparison allows one to predict most of the secondary structures in the PBPs and the amino acid motifs that define the enzyme active sites.

Corrigendum to “Protection of mice against H. somni septicemia by vaccination with recombinant immunoglobulin binding protein subunits” [Vaccine 26 (2008) 4506–4512]

Vaccine ◽  
2012 ◽  
Vol 30 (30) ◽  
pp. 4578
Author(s):  
Roger S. Geertsema ◽  
Carolyn Worby ◽  
Robert P. Kruger ◽  
Yuichi Tagawa ◽  
Riccardo Russo ◽  
...  
Keyword(s):  
Binding Protein ◽  
Protein Subunits ◽  
Immunoglobulin Binding Protein ◽  
Immunoglobulin Binding

Interaction of human complement with Sbi, a staphylococcal immunoglobulin-binding protein

2007 ◽  
Vol 44 (16) ◽  
pp. 3982 ◽  
Author(s):  
Julia Burman ◽  
Elisa Leung ◽  
David E. Isenman ◽  
Jean M.H. van den Elsen
Keyword(s):  
Binding Protein ◽  
Human Complement ◽  
Immunoglobulin Binding Protein ◽  
Immunoglobulin Binding
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