3vl8
Crystal structure of XEG
Structural highlights
FunctionXGEA_ASPAC Catalyzes endohydrolysis of 1,4-beta-D-glucosidic linkages in xyloglucan with retention of the beta-configuration of the glycosyl residues. Specific for xyloglucan and does not hydrolyze other cell wall components.[1] [2] Publication Abstract from PubMedMicroorganisms such as plant pathogens secrete glycoside hydrolases (GHs) to digest the polysaccharide chains of plant cell-walls. The degradation of cell-walls by these enzymes is a crucial step for nutrition and invasion. To protect the cell-wall from these enzymes, plants secrete glycoside hydrolase inhibitor proteins (GHIPs). Xyloglucan-specific endo-beta-1,4-glucanase (XEG), a member of GH family 12 (GH12), could be a great threat to many plants since xyloglucan is a major component of the cell-wall in most plants. Understanding the inhibition mechanism of XEG by GHIP is therefore of great importance in the field of plant defense, but to date the mechanism and specificity of GHIPs remain unclear. We have determined the crystal structure of XEG in complex with extracellular dermal glycoprotein (EDGP), a carrot GHIP that inhibits XEG. The structure reveals that the conserved arginines of EDGP intrude into the active site of XEG and interact with the catalytic glutamates of the enzyme. We have also determined the crystal structure of the XEG-xyloglucan complex. These structures show that EDGP closely mimics the XEG-xyloglucan interaction. Although EDGP shares structural similarity to a wheat GHIP (TAXI-IA) that inhibits GH11 family xylanases, the arrangement of GH and GHIP in the XEG-EDGP complex is distinct from that in the xylanase-TAXI-IA complex. Our findings imply that plants have evolved structures of GHIPs to inhibit different GH family members that attack their cell-walls. Structural basis for the inhibition of xyloglucan-specific endo-beta-1,4-glucanase (XEG) by XEG-protein inhibitor.,Yoshizawa T, Shimizu T, Hirano H, Sato M, Hashimoto H J Biol Chem. 2012 Apr 10. PMID:22496365[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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