1NKG

Rhamnogalacturonan lyase from Aspergillus aculeatus

Summary for 1NKG

• Entry DOI: 10.2210/pdb1nkg/pdb
• Descriptor: Rhamnogalacturonase B, CALCIUM ION, SULFATE ION, ... (4 entities in total)
• Functional Keywords: polysaccharide lyase, carbohydrate active enzyme, pectin, lyase
• Biological source: Aspergillus aculeatus
• Cellular location: Secreted : Q00019
• Total number of polymer chains: 1
• Total formula weight: 54667.85

Authors

McDonough, M.A.,Kadirvelraj, R.,Harris, P.,Poulsen, J.C.,Larsen, S. (deposition date: 2003-01-03, release date: 2004-05-25, Last modification date: 2024-11-06)

Primary citation

McDonough, M.A.,Kadirvelraj, R.,Harris, P.,Poulsen, J.C.,Larsen, S.
Rhamnogalacturonan lyase reveals a unique three-domain modular structure for polysaccharide lyase family 4.
Febs Lett., 565:188-194, 2004

PubMed Abstract: Rhamnogalacturonan lyase (RG-lyase) specifically recognizes and cleaves alpha-1,4 glycosidic bonds between L-rhamnose and D-galacturonic acids in the backbone of rhamnogalacturonan-I, a major component of the plant cell wall polysaccharide, pectin. The three-dimensional structure of RG-lyase from Aspergillus aculeatus has been determined to 1.5 A resolution representing the first known structure from polysaccharide lyase family 4 and of an enzyme with this catalytic specificity. The 508-amino acid polypeptide displays a unique arrangement of three distinct modular domains. Each domain shows structural homology to non-catalytic domains from other carbohydrate active enzymes.

PubMed: 15135077
DOI: 10.1016/j.febslet.2004.03.094

Experimental method

X-RAY DIFFRACTION (1.5 Å)