1x90

Crystal structure of mutant form B of a pectin methylesterase inhibitor from Arabidopsis

spinqualitylabelsall models 1x90, resolution 2.68Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1x90 is a 2 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.68Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PMEI1_ARATH Inhibits pectin methylesterase from flowers and siliques. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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