The Crystal Structure of Helicobacter pylori Cysteine-rich Protein B Reveals a Novel Fold for a Penicillin-binding Protein. Lucas Lu¨ thy, Markus G. Gru¨ tter, and Peer R. E. Mittl JOURNAL OF BIOLOGICAL CHEMISTRY Vol. 277, No. 12, Issue of March 22, pp. 10187–10193, 2002.
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The Crystal Structure of Helicobacter pylori Cysteine-rich Protein BReveals a Novel Fold for a Penicillin-binding Protein
Lucas Lu¨ thy, Markus G. Gru¨ tter, and Peer R. E. Mittl
JOURNAL OF BIOLOGICAL CHEMISTRY
Vol. 277, No. 12, Issue of March 22, pp. 10187–10193, 2002
THE JOURNAL OF BIOLOGICAL CHEMISTRY Vol. 275, No. 23, Issue of June 9, pp. 17693–17699, 2000
Characterization of Folding
CD spectrum of refolded HcpB.
Ellipticity at a wavelength of 222 nm as a function of GdmHCl concentration.
Based on the CD spectrum, the –αhelix content was predicted to be 73%, [GdmHCl]1 /2 values is 1.93 +-0.02 M and free energy is unfolding of -22 kJ/mol.
R.m.s.d. and sequence identity among α / α -motifs of HcpB
Stereo view of the superposition of
four HcpB α / α -motifs.
Residues that are conserved are highlighted
The cysteine residues at positions 20 and 28, alanine at position 19, and glycine at position 27 are conserved for structural reasons.
Throughout the whole Hcp family, residues preceding the cysteines are always glycine, alanine, or serine residues because these residue types possess sufficiently small side chains.
N-acetylmuramic acid (NAM) is a compound that is found in the peptidoglycan of all Gram-negative bacteria.
Water molecules and 2Fo-Fc electron density in the putative ligand binding site.
Modeled N-acetylmuramic acid/HcpB complex..
BioEssays 21:932–939, r 1999 John Wiley & Sons, Inc.
The EMBO Journal Vol.17 No.5 pp.1192–1199, 1998
leucine at position 22 is also conserved in TPR repeats 1 and 2, whereas the lysine and asparagine residues at positions 11, 14, and 18 that are located on the convex surface of HcpB are not.