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1DEO

RHAMNOGALACTURONAN ACETYLESTERASE FROM ASPERGILLUS ACULEATUS AT 1.55 A RESOLUTION WITH SO4 IN THE ACTIVE SITE

Summary for 1DEO
Entry DOI10.2210/pdb1deo/pdb
Related1DEX
DescriptorRHAMNOGALACTURONAN ACETYLESTERASE, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
Functional Keywordssgnh hydrolase, hydrolase
Biological sourceAspergillus aculeatus
Total number of polymer chains1
Total formula weight26109.18
Authors
Molgaard, A.,Kauppinen, S.,Larsen, S. (deposition date: 1999-11-15, release date: 2000-04-26, Last modification date: 2024-11-20)
Primary citationMolgaard, A.,Kauppinen, S.,Larsen, S.
Rhamnogalacturonan acetylesterase elucidates the structure and function of a new family of hydrolases.
Structure Fold.Des., 8:373-383, 2000
Cited by
PubMed Abstract: The complex polysaccharide rhamnogalacturonan constitutes a major part of the hairy region of pectin. It can have different types of carbohydrate sidechains attached to the rhamnose residues in the backbone of alternating rhamnose and galacturonic acid residues; the galacturonic acid residues can be methylated or acetylated. Aspergillus aculeatus produces enzymes that are able to perform a synergistic degradation of rhamnogalacturonan. The deacetylation of the backbone by rhamnogalacturonan acetylesterase (RGAE) is an essential prerequisite for the subsequent action of the enzymes that cleave the glycosidic bonds.
PubMed: 10801485
DOI: 10.1016/S0969-2126(00)00118-0
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.55 Å)
Structure validation

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