1xg2
From Proteopedia
(New page: 200px<br /><applet load="1xg2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xg2, resolution 1.90Å" /> '''Crystal structure of...) |
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| - | [[Image:1xg2.gif|left|200px]]<br /><applet load="1xg2" size=" | + | [[Image:1xg2.gif|left|200px]]<br /><applet load="1xg2" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1xg2, resolution 1.90Å" /> | caption="1xg2, resolution 1.90Å" /> | ||
'''Crystal structure of the complex between pectin methylesterase and its inhibitor protein'''<br /> | '''Crystal structure of the complex between pectin methylesterase and its inhibitor protein'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Pectin, one of the main components of the plant cell wall, is secreted in | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1XG2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Actinidia_chinensis Actinidia chinensis] and [http://en.wikipedia.org/wiki/Solanum_lycopersicum Solanum lycopersicum]. Active as [http://en.wikipedia.org/wiki/Pectinesterase Pectinesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.11 3.1.1.11] Full crystallographic information is available from [http:// | + | 1XG2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Actinidia_chinensis Actinidia chinensis] and [http://en.wikipedia.org/wiki/Solanum_lycopersicum Solanum lycopersicum]. Active as [http://en.wikipedia.org/wiki/Pectinesterase Pectinesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.11 3.1.1.11] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XG2 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Cervone, F.]] | [[Category: Cervone, F.]] | ||
[[Category: Giovane, A.]] | [[Category: Giovane, A.]] | ||
| - | [[Category: Lorenzo, G | + | [[Category: Lorenzo, G De.]] |
| - | [[Category: Matteo, A | + | [[Category: Matteo, A Di.]] |
[[Category: Raiola, A.]] | [[Category: Raiola, A.]] | ||
[[Category: Tsernoglou, D.]] | [[Category: Tsernoglou, D.]] | ||
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[[Category: protein-protein complex]] | [[Category: protein-protein complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:54:25 2008'' |
Revision as of 13:54, 21 February 2008
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Crystal structure of the complex between pectin methylesterase and its inhibitor protein
Overview
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.
About this Structure
1XG2 is a Protein complex structure of sequences from Actinidia chinensis and Solanum lycopersicum. Active as Pectinesterase, with EC number 3.1.1.11 Full crystallographic information is available from OCA.
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:15722470
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