First published online February 18, 2005; 10.1105/tpc.104.028886
The Plant Cell 17:849-858 (2005)
© 2005 American Society of Plant Biologists
Structural Basis for the Interaction between Pectin Methylesterase and a Specific Inhibitor Protein
Adele Di Matteoa,b,
Alfonso Giovanec,
Alessandro Raiolab,1,
Laura Camardellad,
Daniele Boniventoa,
Giulia De Lorenzob,
Felice Cervoneb,
Daniela Bellincampib,2 and
Demetrius Tsernogloua
a Department of Biochemical Sciences, University of Rome, 00185 Rome, Italy
b Department of Plant Biology, University of Rome, 00185 Rome, Italy
c Department of Biochemistry and Biophysics, Second University of Naples, I-80138, Naples, Italy
d Institute of Protein Biochemistry, Consiglio Nazionale delle Ricerche, I-80125, Naples, Italy
2 To whom correspondence should be addressed. E-mail daniela.bellincampi{at}uniroma1.it; fax 39-06-49912446.
Pectin, one of the main components of the plant cell wall, is secreted in a highly methyl-esterified form and subsequently deesterified in muro by pectin methylesterases (PMEs). In many developmental processes, PMEs are regulated by either differential expression or posttranslational control by protein inhibitors (PMEIs). PMEIs are typically active against plant PMEs and ineffective against microbial enzymes. Here, we describe the three-dimensional structure of the complex between the most abundant PME isoform from tomato fruit (Lycopersicon esculentum) and PMEI from kiwi (Actinidia deliciosa) at 1.9-Å resolution. The enzyme folds into a right-handed parallel ß-helical structure typical of pectic enzymes. The inhibitor is almost all helical, with four long  -helices aligned in an antiparallel manner in a classical up-and-down four-helical bundle. The two proteins form a stoichiometric 1:1 complex in which the inhibitor covers the shallow cleft of the enzyme where the putative active site is located. The four-helix bundle of the inhibitor packs roughly perpendicular to the main axis of the parallel ß-helix of PME, and three helices of the bundle interact with the enzyme. The interaction interface displays a polar character, typical of nonobligate complexes formed by soluble proteins. The structure of the complex gives an insight into the specificity of the inhibitor toward plant PMEs and the mechanism of regulation of these enzymes.
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