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 §1§ The ι-Carrageenase of Alteromonas fortis §1§

 §2§ A β-HELIX FOLD-CONTAINING ENZYME FOR THE DEGRADATION OF A HIGHLY
POLYANIONIC POLYSACCHARIDE[15]* §2§

    1. [16]Gurvan Michel[17]‡[18]§,
    2. [19]Laurent Chantalat[20]‡,
    3. [21]Eric Fanchon[22]‡,
    4. [23]Bernard Henrissat[24]¶,
    5. [25]Bernard Kloareg[26]§ and
    6. [27]Otto Dideberg[28]‡[29]‖

    1.


    From the ^‡Laboratoire de Cristallographie Macromoléculaire, Institut
    de Biologie Structurale Jean-Pierre Ebel, CNRS/Commissariat Ã…
    l'Energie Atomique, 41, rue Jules Horowitz, 38027 Grenoble Cedex 1,
    France, the ^§Station Biologique de Roscoff, UMR 1931 (CNRS and
    Laboratoires Goëmar), Place Georges Teissier, BP 74, 29682 Roscoff
    Cedex, France, and the ^¶Architecture et Fonction des Macromolécules
    Biologiques, UMR 6098 (CNRS, Universités d'Aix-Marseille I et II), 31
    Chemin Joseph Aiguier, 13402 Marseille Cedex 20, France


   [30]Next Section

 §2§ Abstract §2§

   Carrageenans are gel-forming hydrocolloids extracted from the cell
   walls of marine red algae. They consist ofd-galactose residues bound by
   alternate α(1→3) and β(1→4) linkages and substituted by one
   (κ-carrageenan), two (ι-carrageenan), or three (λ-carrageenan)
   sulfate-ester groups per disaccharide repeating unit. Both the κ- and
   ι-carrageenan chains adopt ordered conformations leading to the
   formation of highly ordered aggregates of double-stranded helices.
   Several κ-carrageenases and ι-carrageenases have been cloned from
   marine bacteria. κ-Carrageenases belong to family 16 of the glycoside
   hydrolases, which essentially encompasses polysaccharidases specialized
   in the hydrolysis of the neutral polysaccharides such as agarose,
   laminarin, lichenan, and xyloglucan. In contrast, ι-carrageenases
   constitute a novel glycoside hydrolase structural family. We report
   here the crystal structure of Alteromonas fortisι-carrageenase at 1.6 Å
   resolution. The enzyme folds into a right-handed parallel β-helix of 10
   complete turns with two additional C-terminal domains. Glu^245,
   Asp^247, or Glu^310, in the cleft of the enzyme, are proposed as
   candidate catalytic residues. The protein contains one sodium and one
   chloride binding site and three calcium binding sites shown to be
   involved in stabilizing the enzyme structure.

   Carrageenans are the main components of the cell walls of various
   marine red algae (Rhodophyta) where they play a variety of structural
   (cell-cell cohesion and exchange boundary) and signaling (cell-cell
   recognition) roles ([31]1, [32]2). They consist of linear chains of
   galactopyranose residues in the d-configuration linked by alternating
   α(1→3) and β(1→4) linkages. This regular structure is modified by
   3,6-anhydro bridges and substitution with sulfate-ester groups. On the
   basis of the level and position of sulfate substitution, carrageenans
   are classified into four types, namely furcellaran and κ-, ι-, and
   λ-carrageenans. κ-Carrageenan consists of repeated units of the
   disaccharide
   4-sulfate-O-1,3-β-d-galactopyranosyl-1,4-α-3,6-anhydro-d-galactose,
   also known as neocarrabiose sulfate. At the primary structure level,
   ι-carrageenan differs from κ-carrageenan in the presence at C-2 on the
   α-linked galactose residues of one additional sulfate substituent per
   repeating disaccharide (Fig.[33]1). ι-Carrageenans therefore contain
   two sulfate groups per repeat unit, i.e. one anionic group per
   monosaccharide. Such a high linear charge density is reminiscent of
   that seen in alginic acid, the main cell wall polysaccharide of brown
   algae, and in polygalacturonic acid, the nonmethylated component of
   higher plant pectins, which both contain one carboxyl group per
   monomeric unit ([34]1).
   [35]Figure 1
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   protein expression, Dr. Anne-Marie DiGuilmi for precious help with the
   proteolysis analysis, and Dr. Tristan Barbeyron for helpful discussion.
   [150]Previous Section[151]Next Section

 §2§ Footnotes §2§

     * [152]↵* This work was supported by grants from the Action Concertée
       Coordonnée Sciences du Vivant (No. V) and Groupement de Rechereches
       1002 of CNRS “Biology, Biochemistry and Genetics of Marine
       Algae.”The costs of publication of this article were defrayed in
       part by the payment of page charges. The 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 the structure factors (code ) have been
       deposited in the Protein Data Bank, Research Collaboratory for
       Structural Bioinformatics, Rutgers University, New Brunswick, NJ
       ([153]http://www.rcsb.org/).
     * [154]↵‖ To whom correspondence should be addressed. Tel.:
       33-4-38-78-56-09; Fax: 33-4-38-78-54-94; E-mail: otto@ibs.fr.
     * Published, JBC Papers in Press, August 7, 2001, DOI
       10.1074/jbc.M100670200
     * Abbreviations:

        Se-Met
                seleno-l-methionine

     *
          + Received January 24, 2001.
          + Revision received June 13, 2001.
     * The American Society for Biochemistry and Molecular Biology, Inc.

   [155]Previous Section

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