HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 277, Issue 12, 10187-10193, March 22, 2002

This Article Full Text Full Text (PDF) All Versions of this Article: 277/12/10187    most recent M108993200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Lüthy, L. Articles by Mittl, P. R. E. Search for Related Content PubMed PubMed Citation Articles by Lüthy, L. Articles by Mittl, P. R. E. Social Bookmarking                      What's this?

The Crystal Structure of Helicobacter pylori Cysteine-rich Protein B Reveals a Novel Fold for a Penicillin-binding Protein^*

Lucas Lüthy, Markus G. Grütter, and Peer R. E. Mittl

From the Biochemisches Institut, Universität Zürich, Winterthurer Strasse 190, 8057 Zürich, Switzerland

Colonization of the gastric mucosa with the spiral-shaped Gram-negative proteobacterium Helicobacter pylori is probably the most common chronic infection in humans. The genomes of H. pylori strains J99 and 26695 have been completely sequenced. Functional and three-dimensional structural information is available for less than one third of all open reading frames. We investigated the function and three-dimensional structure of a member from a family of cysteine-rich hypothetical proteins that are unique to H. pylori and Campylobacter jejuni. The structure of H. pylori cysteine-rich protein (Hcp) B possesses a modular architecture consisting of four /-motifs that are cross-linked by disulfide bridges. The Hcp repeat is similar to the tetratricopeptide repeat, which is frequently found in protein/protein interactions. In contrast to the tetratricopeptide repeat, the Hcp repeat is 36 amino acids long. HcpB is capable of binding and hydrolyzing 6-amino penicillinic acid and 7-amino cephalosporanic acid derivatives. The HcpB fold is distinct from the fold of any known penicillin-binding protein, indicating that the Hcp proteins comprise a new family of penicillin-binding proteins. The putative penicillin binding site is located in an amphipathic groove on the concave side of the molecule.

The atomic coordinates and the structure factors (code 1KLX) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				L. Deml, M. Aigner, J. Decker, A. Eckhardt, C. Schutz, P. R. E. Mittl, S. Barabas, S. Denk, G. Knoll, N. Lehn, et al. Characterization of the Helicobacter pylori Cysteine-Rich Protein A as a T-Helper Cell Type 1 Polarizing Agent Infect. Immun., August 1, 2005; 73(8): 4732 - 4742. [Abstract] [Full Text] [PDF]

				M. Suzuki, A. Neutzner, N. Tjandra, and R. J. Youle Novel Structure of the N Terminus in Yeast Fis1 Correlates with a Specialized Function in Mitochondrial Fission J. Biol. Chem., June 3, 2005; 280(22): 21444 - 21452. [Abstract] [Full Text] [PDF]

				P. R. E. Mittl, L. Luthy, C. Reinhardt, and H. Joller Detection of High Titers of Antibody against Helicobacter Cysteine-Rich Proteins A, B, C, and E in Helicobacter pylori-Infected Individuals Clin. Vaccine Immunol., July 1, 2003; 10(4): 542 - 545. [Abstract] [Full Text] [PDF]

				R. K. Deka, M. Machius, M. V. Norgard, and D. R. Tomchick Crystal Structure of the 47-kDa Lipoprotein of Treponema pallidum Reveals a Novel Penicillin-binding Protein J. Biol. Chem., October 25, 2002; 277(44): 41857 - 41864. [Abstract] [Full Text] [PDF]