Structural requirements of
            <i>endo</i>
            polygalacturonase for the interaction with PGIP (polygalacturonase-inhibiting protein)

Federici, L.; Caprari, Claudio; Mattei, Benedetta; Savino, C.; Matteo, Adele Di; Lorenzo, Giulia De; Cervone, Felice; Tsernoglou, Demetrius

doi:10.1073/pnas.231473698

Cited by 134 publications

(142 citation statements)

References 44 publications

(44 reference statements)

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“…Letters following T identify the position of each turn with respect to the coil of the b-helix, whereas A corresponds to the first turn in the N-terminal region. Turns T1 (except for TB1) are short and mainly composed of residues in a L -conformation and are responsible for the sharp bend between the sheets as observed in other parallel b-helix structures (Federici et al, 2001;. Turns T2 and T3 are generally longer and more variable; in particular, TF3 and most of T2 turns protrude from the central parallel b-helix to form the shallow cleft where the putative active site is located.…”

Section: Resultsmentioning

confidence: 93%

Structural Basis for the Interaction between Pectin Methylesterase and a Specific Inhibitor Protein

Matteo¹,

Giovane

Raiola³

et al. 2005

Plant Cell

201

224

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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 b-helical structure typical of pectic enzymes. The inhibitor is almost all helical, with four long a-helices aligned in an antiparallel manner in a classical up-and-down fourhelical 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 b-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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Section: Resultsmentioning

confidence: 93%

Structural Basis for the Interaction between Pectin Methylesterase and a Specific Inhibitor Protein

Matteo¹,

Giovane

Raiola³

et al. 2005

Plant Cell

201

224

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“…By careful inspection of the Hbonding pattern, B2 may be considered a single sheet formed by the clustering of four shorter sheets that interact together. The presence of the additional sheet B2 places the fold of PGIP2 between the typical LRR structure and the ␤-helical architecture found in pectate lyases and PGs that contain three to four ␤-sheets (30)(31)(32)(33). PGIP2 belongs to the plant-specific LRR subfamily characterized by the consensus sequence Lt͞sGxIP in the region following the conserved ''␤-structure ϩ Asn-ladder'' (23).…”

Section: Resultsmentioning

confidence: 99%

The crystal structure of polygalacturonase-inhibiting protein (PGIP), a leucine-rich repeat protein involved in plant defense

Matteo¹,

Federici²,

Mattei³

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

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204

273

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Polygalacturonase-inhibiting proteins (PGIPs) are plant cell wall proteins that protect plants from fungal invasion. They interact with endopolygalacturonases secreted by phytopathogenic fungi, inhibit their enzymatic activity, and favor the accumulation of oligogalacturonides, which activate plant defense responses. PGIPs are members of the leucine-rich repeat (LRR) protein family that in plants play crucial roles in development, defense against pathogens, and recognition of beneficial microbes. Here we report the crystal structure at 1.7-Å resolution of a PGIP from Phaseolus vulgaris. The structure is characterized by the presence of two ␤-sheets instead of the single one originally predicted by modeling studies. The structure also reveals a negatively charged surface on the LRR concave face, likely involved in binding polygalacturonases. The structural information on PGIP provides a basis for designing more efficient inhibitors for plant protection.

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“…Extracellular LRRs are also found in receptor-like kinases and it is possible that PGIPs evolved from these LRR proteins by truncation and subsequent specialization. The crystal structure of F. moniliforme FmPG1 showed that this protein has two additional loops that form a lid over the active site, causing the substrate-binding cleft to become narrower [28]. This lid is absent in other PGs, such as B. cinerea BcPG1 [29 ], and may have evolved to prevent binding of substrate-mimicking inhibitors.…”

Section: Wheat Inhibitor Xip-i Targets Fungal Gh11 and Gh10 Xylanasesmentioning

confidence: 99%

Enzyme–inhibitor interactions at the plant–pathogen interface

Misas-Villamil

Hoorn

2008

Current Opinion in Plant Biology

115

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The plant apoplast during plant-pathogen interactions is an ancient battleground that holds an intriguing range of attacking enzymes and counteracting inhibitors. Examples are pathogen xylanases and polygalacturonases that are inhibited by plant proteins like TAXI, XIP, and PGIP; and plant glucanases and proteases, which are targeted by pathogen proteins such as GIP1, EPI1, EPIC2B, and AVR2. These seven well-characterized inhibitors have different modes of action and many probably evolved from inactive enzymes themselves. Detailed studies of the structures, sequence variation, and mutated proteins uncovered molecular struggles between these enzymes and their inhibitors, resulting in positive selection for variant residues at the contact surface, where single residues determine the outcome of the interaction. Introduction Extracellular plant-pathogen interactions probably existed long before the evolution of pathogen effector translocation systems and plant resistance (R) genes. The molecular basis of these interactions is mostly undiscovered but some have been investigated in detail and reveal intriguing mechanisms. Here we will highlight major recent findings of extracellular enzyme-inhibitor interactions at the plant-pathogen interface.Although extracellular plant-pathogen interactions are complex, they can be simplified by assuming that they evolved in several stages (Figure 1). First, micro-organisms became pathogens by attacking plants using cell-wall-degrading enzymes and other hydrolases ( Figure 1A). In response to this attack, plants secrete inhibitors that suppress these hydrolases ( Figure 1B). Initially, these inhibitors were probably constitutively produced, but upon evolution of pathogen recognition systems the production and secretion of these proteins became inducible, becoming part of the arsenal of pathogenesis-related (PR) proteins. Besides suppression of pathogen attack, counter attack mechanisms also evolved in plants through the induced secretion of hydrolytic enzymes ( Figure 1C). Examples are the well-studied PR proteins including endo-b-1,3-glucanases (PR-2), chitinases (PR-3), and proteases (PR-7) [1 ]. Pathogens, in turn, responded to this counter attack by producing inhibitors that suppress these enzymes ( Figure 1D). The fifth and latest step was a sophisticated refinement of the pathogen recognition system by the evolution of R genes that recognize the manipulation of plant targets by pathogens, inducing a severe defense response that includes cell death ( Figure 1E). Aspects of this simplified model are consistent with the 'zigzag' model for the plant immune system, which explains the suppression of basal defense responses by pathogen effector proteins, followed by the evolution of efficient effector recognition by R proteins [2].Antagonistic interactions between organisms at the molecular level result in enzymes that evade inhibition, and inhibitors that adapt to these new enzymes. These 'molecular struggles' result in positive selection for variation of residues at the interactio...

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Structural requirements of endo polygalacturonase for the interaction with PGIP (polygalacturonase-inhibiting protein)

Cited by 134 publications

References 44 publications

Structural Basis for the Interaction between Pectin Methylesterase and a Specific Inhibitor Protein

Structural Basis for the Interaction between Pectin Methylesterase and a Specific Inhibitor Protein

The crystal structure of polygalacturonase-inhibiting protein (PGIP), a leucine-rich repeat protein involved in plant defense

Enzyme–inhibitor interactions at the plant–pathogen interface

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