1ee6
From Proteopedia
CRYSTAL STRUCTURE OF PECTATE LYASE FROM BACILLUS SP. STRAIN KSM-P15.
Overview
The crystal structure of a highly alkaline low molecular weight pectate lyase (Pel-15) was determined at 1.5 A resolution by the multiple isomorphous replacement (MIR) method. This is the first pectate lyase structure from polysaccharide lyase family 3. The overall structure is a simple eight-turn right-handed parallel beta-helix domain with one long loop protruding from one side of the beta-helix. The low molecular weight of Pel-15 derives from the lack of N- and C-terminal extensions that are found in many beta-helix proteins. Although the structure has one calcium ion at pH 6.7, raising the pH to 9.5 results in the binding of an additional calcium ion. The common calcium ion found in both the pH 6.5 and 9.5 structures seems to stabilize both the beta-helix structure and the long protruding loop. The additional calcium ion found in the pH 9.5 structure alone may neutralize the acidic substrate. The region around the additional calcium ion is thought to bind to the substrate, as this region is rich in charged amino-acid residues which are required in catalysis.
About this Structure
1EE6 is a Single protein structure of sequence from Bacillus sp.. Full crystallographic information is available from OCA.
Reference
The first structure of pectate lyase belonging to polysaccharide lyase family 3., Akita M, Suzuki A, Kobayashi T, Ito S, Yamane T, Acta Crystallogr D Biol Crystallogr. 2001 Dec;57(Pt 12):1786-92. Epub 2001, Nov 21. PMID:11717490 Page seeded by OCA on Fri May 2 14:59:14 2008
