THE STRUCTURE OF BACILLUS-SUBTILIS PECTATE LYASE IN COMPLEX WITH CALCIUM

Citation
R. Pickersgill et al., THE STRUCTURE OF BACILLUS-SUBTILIS PECTATE LYASE IN COMPLEX WITH CALCIUM, Nature structural biology, 1(10), 1994, pp. 717-723
Citations number
18
Categorie Soggetti
Biology,"Cell Biology
Journal title
ISSN journal
10728368
Volume
1
Issue
10
Year of publication
1994
Pages
717 - 723
Database
ISI
SICI code
1072-8368(1994)1:10<717:TSOBPL>2.0.ZU;2-#
Abstract
We have solved the structure of the Bacillus subtilis pectate lyase (B sPel) in complex with calcium, The structure consists of a parallel be ta-helix domain and a loop region. The alpha(L)-bounded beta-strand se en in BsPel is a new element of protein structure and its frequent occ urrence suggests it is an important characteristic of the parallel bet a-helix, A pronounced cleft is formed between the loops and the parall el beta-helix domain and we propose that this is the active site deft. Calcium, essential for the activity of the enzyme, binds at the botto m of this cleft and an arginine residue dose to the calcium, which is conserved across all pectin and pectate lyases, may be involved in cat alysis.