1xg2: Difference between revisions

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[[Image:1xg2.gif|left|200px]]
{{Seed}}
[[Image:1xg2.png|left|200px]]


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{{STRUCTURE_1xg2|  PDB=1xg2  |  SCENE=  }}  
{{STRUCTURE_1xg2|  PDB=1xg2  |  SCENE=  }}  


'''Crystal structure of the complex between pectin methylesterase and its inhibitor protein'''
===Crystal structure of the complex between pectin methylesterase and its inhibitor protein===




==Overview==
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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-A resolution. The enzyme folds into a right-handed parallel beta-helical structure typical of pectic enzymes. The inhibitor is almost all helical, with four long alpha-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 beta-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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{{ABSTRACT_PUBMED_15722470}}


==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Structural basis for the interaction between pectin methylesterase and a specific inhibitor protein., Di Matteo A, Giovane A, Raiola A, Camardella L, Bonivento D, De Lorenzo G, Cervone F, Bellincampi D, Tsernoglou D, Plant Cell. 2005 Mar;17(3):849-58. Epub 2005 Feb 18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15722470 15722470]
Structural basis for the interaction between pectin methylesterase and a specific inhibitor protein., Di Matteo A, Giovane A, Raiola A, Camardella L, Bonivento D, De Lorenzo G, Cervone F, Bellincampi D, Tsernoglou D, Plant Cell. 2005 Mar;17(3):849-58. Epub 2005 Feb 18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15722470 15722470]
Pectin methylesterase inhibitor., Giovane A, Servillo L, Balestrieri C, Raiola A, D'Avino R, Tamburrini M, Ciardiello MA, Camardella L, Biochim Biophys Acta. 2004 Feb 12;1696(2):245-52. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14871665 14871665]
Tomato pectin methylesterase: modeling, fluorescence, and inhibitor interaction studies-comparison with the bacterial (Erwinia chrysanthemi) enzyme., D'Avino R, Camardella L, Christensen TM, Giovane A, Servillo L, Proteins. 2003 Dec 1;53(4):830-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14635125 14635125]
Pectin methylesterases: cell wall enzymes with important roles in plant physiology., Micheli F, Trends Plant Sci. 2001 Sep;6(9):414-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11544130 11544130]
[[Category: Actinidia chinensis]]
[[Category: Actinidia chinensis]]
[[Category: Pectinesterase]]
[[Category: Pectinesterase]]
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[[Category: Beta helix,four helix bundle]]
[[Category: Beta helix,four helix bundle]]
[[Category: Protein-protein complex]]
[[Category: Protein-protein complex]]
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