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J. Biol. Chem., Vol. 279, Issue 29, 30395-30401, July 16, 2004

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The Structure of the Cys-rich Terminal Domain of Hydra Minicollagen, Which Is Involved in Disulfide Networks of the Nematocyst Wall^*

Elena Pokidysheva, Alexander G. Milbradt¶, Sebastian Meier||, Christian Renner¶, Daniel Häussinger||, Hans Peter Bächinger**, Luis Moroder¶, Stephan Grzesiek||, Thomas W. Holstein, Suat Özbek¶¶, and Jürgen Engel

From the Department of Biophysical Chemistry, Biozentrum, University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland, the ^¶Max Planck Institute for Biochemistry, D-82152 Martinsried, Germany, the ^||Department of Structural Biology, Biozentrum, University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland, the ^**Shriners Hospital for Children and Department of Biochemistry and Molecular Biology, Oregon Health and Science University, Portland, Oregon 97239, and the Institute of Zoology, Technical University of Darmstadt, Schnittpahnstrasse 10, D-64287 Darmstadt, Germany

The minicollagens found in the nematocysts of Hydra constitute a family of invertebrate collagens with unusual properties. They share a common modular architecture with a central collagen sequence ranging from 14 to 16 Gly-X-Y repeats flanked by polyproline/hydroxyproline stretches and short terminal domains that show a conserved cysteine pattern (CXXXCXXXCXXX-CXXXCC). The minicollagen cysteine-rich domains are believed to function in a switch of the disulfide connectivity from intra- to intermolecular bonds during maturation of the capsule wall. The solution structure of the C-terminal fragment including a minicollagen cysteine-rich domain of minicollagen-1 was determined in two independent groups by ¹H NMR. The corresponding peptide comprising the last 24 residues of the molecule was produced synthetically and refolded by oxidation under low protein concentrations. Both presented structures are identical in their fold and disulfide connections (Cys²-Cys¹⁸, Cys⁶-Cys¹⁴, and Cys¹⁰-Cys¹⁹) revealing a robust structural motif that is supposed to serve as the polymerization module of the nematocyst capsule.

Received for publication, April 5, 2004 , and in revised form, April 22, 2004.

^* This work was supported by Swiss National Science Foundation (SNF) Grant 31-61'757.00 (to S. G.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The atomic coordinates and structure factors (codes 1SP7 and 1SOP) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

These authors contributed equally to this work.

To whom correspondence may be addressed. E-mail: stephan.grzesiek{at}unibas.ch. ¶¶ To whom correspondence may be addressed. E-mail: suat.oezbek{at}unibas.ch.

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