1pp4 | pdb_00001pp4
The crystal structure of rhamnogalacturonan acetylesterase in space group P3121
| |||||||||||||
| 1pp4, resolution 2.5Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Ligands: | NAG | ||||||||||||
| Gene: | RHA1 (Aspergillus aculeatus) | ||||||||||||
| Related: | 1DEO, 1DEX, 1K7C
| ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Overview
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.
About this Structure
1PP4 is a Single protein structure of sequence from Aspergillus aculeatus. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Sun Mar 30 23:02:40 2008
