1DEX

RHAMNOGALACTURONAN ACETYLESTERASE FROM ASPERGILLUS ACULEATUS AT 1.9 A RESOLUTION

Summary for 1DEX

• Entry DOI: 10.2210/pdb1dex/pdb
• Related: 1DEO
• Descriptor: RHAMNOGALACTURONAN ACETYLESTERASE, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-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, ... (4 entities in total)
• Functional Keywords: sgnh hydrolase, hydrolase
• Biological source: Aspergillus aculeatus
• Total number of polymer chains: 1
• Total formula weight: 25917.05

Authors

Molgaard, A.,Kauppinen, S.,Larsen, S. (deposition date: 1999-11-16, release date: 2000-04-26, Last modification date: 2024-10-30)

Primary citation

Molgaard, 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

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

Experimental method

X-RAY DIFFRACTION (1.9 Å)