3vlb

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Template:STRUCTURE 3vlb

Contents

Crystal structure of xeg-edgp

Template:ABSTRACT PUBMED 22496365

Function

[XGEA_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]

About this Structure

3vlb is a 4 chain structure with sequence from Aspergillus aculeatus and Daucus carota. Full crystallographic information is available from OCA.

See Also

Reference

  • Yoshizawa T, Shimizu T, Hirano H, Sato M, Hashimoto H. Structural basis for the inhibition of xyloglucan-specific endo-beta-1,4-glucanase (XEG) by XEG-protein inhibitor. J Biol Chem. 2012 Apr 10. PMID:22496365 doi:10.1074/jbc.M112.350520
  1. Pauly M, Andersen LN, Kauppinen S, Kofod LV, York WS, Albersheim P, Darvill A. A xyloglucan-specific endo-beta-1,4-glucanase from Aspergillus aculeatus: expression cloning in yeast, purification and characterization of the recombinant enzyme. Glycobiology. 1999 Jan;9(1):93-100. PMID:9884411
  2. Park YW, Baba K, Furuta Y, Iida I, Sameshima K, Arai M, Hayashi T. Enhancement of growth and cellulose accumulation by overexpression of xyloglucanase in poplar. FEBS Lett. 2004 Apr 23;564(1-2):183-7. PMID:15094064 doi:10.1016/S0014-5793(04)00346-1

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