1NHC

Structural insights into the processivity of endopolygalacturonase I from Aspergillus niger

Summary for 1NHC

• Entry DOI: 10.2210/pdb1nhc/pdb
• Related: 1CZF
• Descriptor: Polygalacturonase I, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 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, ... (9 entities in total)
• Functional Keywords: beta-helix, hydrolase
• Biological source: Aspergillus niger
• Cellular location: Secreted (Probable): P26213
• Total number of polymer chains: 6
• Total formula weight: 216075.80

Authors

van Pouderoyen, G.,Snijder, H.J.,Benen, J.A.,Dijkstra, B.W. (deposition date: 2002-12-19, release date: 2003-11-25, Last modification date: 2024-12-25)

Primary citation

van Pouderoyen, G.,Snijder, H.J.,Benen, J.A.,Dijkstra, B.W.
Structural insights into the processivity of endopolygalacturonase I from Aspergillus niger.
Febs Lett., 554:462-466, 2003

PubMed Abstract: Endopolygalacturonase I is a processive enzyme, while the 60% sequence identical endopolygalacturonase II is not. The 1.70 A resolution crystal structure of endopolygalacturonase I reveals a narrowed substrate binding cleft. In addition, Arg96, a residue in this cleft previously shown to be critical for processivity, interacts with the substrate mimics glycerol and sulfate in several well-defined conformations in the six molecules in the asymmetric unit. From this we conclude that both Arg96 and the narrowed substrate binding cleft contribute to retaining the substrate while it moves through the active site after a cleavage event has occurred.

PubMed: 14623112
DOI: 10.1016/S0014-5793(03)01221-3

Experimental method

X-RAY DIFFRACTION (1.7 Å)