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

被引：186

作者：

PICKERSGILL, R ^{[1
]}

JENKINS, J ^{[1
]}

HARRIS, G ^{[1
]}

NASSER, W ^{[1
]}

ROBERTBAUDOUY, J ^{[1
]}

机构：

[1] INST NATL SCI APPL,GENET MOLEC MICROORGANISMES LAB,F-69621 VILLEURBANNE,FRANCE

来源：

NATURE STRUCTURAL BIOLOGY | 1994年 / 1卷 / 10期

关键词：

D O I：

10.1038/nsb1094-717

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 deft. Calcium, essential for the activity of the enzyme, binds at the bottom of this cleft and an arginine residue dose to the calcium, which is conserved across all pectin and pectate lyases, may be involved in catalysis.

引用

页码：717 / 723

页数：7

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