1BN8

BACILLUS SUBTILIS PECTATE LYASE

Summary for 1BN8

• Entry DOI: 10.2210/pdb1bn8/pdb
• Descriptor: PROTEIN (PECTATE LYASE), CALCIUM ION (3 entities in total)
• Functional Keywords: parallel beta-helix, lyase
• Biological source: Bacillus subtilis
• Cellular location: Secreted: P39116
• Total number of polymer chains: 1
• Total formula weight: 45587.87

Authors

Pickersgill, R.,Harris, G.,Jenkins, J. (deposition date: 1998-07-31, release date: 1998-08-05, Last modification date: 2024-02-07)

Primary citation

Pickersgill, R.,Jenkins, J.,Harris, G.,Nasser, W.,Robert-Baudouy, J.
The structure of Bacillus subtilis pectate lyase in complex with calcium.
Nat.Struct.Biol., 1:717-723, 1994

PubMed Abstract: We have solved the structure of the Bacillus subtilis pectate lyase (BsPel) in complex with calcium. The structure consists of a parallel beta-helix domain and a loop region. The alpha L-bounded beta-strand seen in BsPel is a new element of protein structure and its frequent occurrence suggests it is an important characteristic of the parallel beta-helix. A pronounced cleft is formed between the loops and the parallel beta-helix domain and we propose that this is the active site cleft. Calcium, essential for the activity of the enzyme, binds at the bottom of this cleft and an arginine residue close to the calcium, which is conserved across all pectin and pectate lyases, may be involved in catalysis.

PubMed: 7634076
DOI: 10.1038/nsb1094-717

Experimental method

X-RAY DIFFRACTION (1.8 Å)