1pp4 | pdb_00001pp4

The crystal structure of rhamnogalacturonan acetylesterase in space group P3121

spinqualitylabelsall models 1pp4, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1pp4 is a 2 chain structure with sequence from Aspergillus aculeatus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.5Å Ligands: NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RHA1_ASPAC Plays a key role in the degradation of rhamnogalacturonan in the cell wall. Acts in synergy together with rhamnogalacturonase A (RGase A) and rhamnogalacturonase B (RGase B). 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 The glycoprotein rhamnogalacturonan acetylesterase from Aspergillus aculeatus has been crystallized in two crystal forms, an orthorhombic and a trigonal crystal form. In the orthorhombic crystal form, the covalently bound carbohydrate at one of the two N-glycosylation sites is involved in crystal contacts. The orthorhombic crystal form was obtained at pH 5.0 and the trigonal crystal form at pH 4.5. In one case, the two crystal forms were found in the same drop at pH 4.7. The differences in crystal packing in the two crystal forms can be explained by the pH-dependent variation in the protonation state of the glutamic acid residues on the protein surface. Crystal packing in two pH-dependent crystal forms of rhamnogalacturonan acetylesterase.,Molgaard A, Larsen S Acta Crystallogr D Biol Crystallogr. 2004 Mar;60(Pt 3):472-8. Epub 2004, Feb 25. PMID:14993671 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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