1x91: Difference between revisions

Revision as of 11:05, 28 July 2008

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File:1x91.png

Template:STRUCTURE 1x91

Crystal structure of mutant form A of a pectin methylesterase inhibitor from ArabidopsisCrystal structure of mutant form A of a pectin methylesterase inhibitor from Arabidopsis

Template:ABSTRACT PUBMED 15528298

About this StructureAbout this Structure

1X91 is a Single protein structure of sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA.

ReferenceReference

Structural insights into the target specificity of plant invertase and pectin methylesterase inhibitory proteins., Hothorn M, Wolf S, Aloy P, Greiner S, Scheffzek K, Plant Cell. 2004 Dec;16(12):3437-47. Epub 2004 Nov 4. PMID:15528298

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OCA

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-'''Crystal structure of mutant form A of a pectin methylesterase inhibitor from Arabidopsis'''
+===Crystal structure of mutant form A of a pectin methylesterase inhibitor from Arabidopsis===
-==Overview==
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-Pectin methylesterase (PME) and invertase are key enzymes in plant carbohydrate metabolism. Inhibitors of both enzymes constitute a sequence family of extracellular proteins. Members of this family are selectively targeted toward either PME or invertase. In a comparative structural approach we have studied how this target specificity is implemented on homologous sequences. By extending crystallographic work on the invertase inhibitor Nt-CIF to a pectin methylesterase inhibitor (PMEI) from Arabidopsis thaliana, we show an alpha-helical hairpin motif to be an independent and mobile structural entity in PMEI. Removal of this hairpin fully inactivates the inhibitor. A chimera composed of the alpha-hairpin of PMEI and the four-helix bundle of Nt-CIF is still active against PME. By contrast, combining the corresponding segment of Nt-CIF with the four-helix bundle of PMEI renders the protein inactive toward either PME or invertase. Our experiments provide insight in how these homologous inhibitors can make differential use of similar structural modules to achieve distinct functions. Integrating our results with previous findings, we present a model for the PME-PMEI complex with important implications.
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