1IDJ

PECTIN LYASE A

Summary for 1IDJ

• Entry DOI: 10.2210/pdb1idj/pdb
• Descriptor: PECTIN LYASE A (2 entities in total)
• Functional Keywords: lyase, glycoprotein, multigene family
• Biological source: Aspergillus niger
• Cellular location: Secreted (Probable): Q01172
• Total number of polymer chains: 2
• Total formula weight: 75918.43

Authors

Mayans, O.,Scott, M.,Connerton, I.,Gravesen, T.,Benen, J.,Visser, J.,Pickersgill, R.,Jenkins, J. (deposition date: 1996-10-04, release date: 1997-10-15, Last modification date: 2024-11-06)

Primary citation

Mayans, O.,Scott, M.,Connerton, I.,Gravesen, T.,Benen, J.,Visser, J.,Pickersgill, R.,Jenkins, J.
Two crystal structures of pectin lyase A from Aspergillus reveal a pH driven conformational change and striking divergence in the substrate-binding clefts of pectin and pectate lyases.
Structure, 5:677-689, 1997

PubMed Abstract: Microbial pectin and pectate lyases are virulence factors that degrade the pectic components of the plant cell wall. The homogalacturan backbone of pectin varies in its degree of methylation from the highly methylated and relatively hydrophobic form known as pectin, to the fully demethylated and highly charged form known as pectate. Methylated and demethylated regions of pectin are cleaved by pectin lyase and calcium-dependent pectate lyases, respectively. Protein engineering of lyases specific for particular patterns of methylation, will yield modified pectins of high value to the food and pharmaceutical industries.

PubMed: 9195887
DOI: 10.1016/S0969-2126(97)00222-0

Experimental method

X-RAY DIFFRACTION (2.4 Å)