1bn8
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(New page: 200px<br /><applet load="1bn8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bn8, resolution 1.8Å" /> '''BACILLUS SUBTILIS PEC...)
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Revision as of 09:38, 20 November 2007
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BACILLUS SUBTILIS PECTATE LYASE
Overview
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.
About this Structure
1BN8 is a Single protein structure of sequence from Bacillus subtilis with CA as ligand. Active as Pectate lyase, with EC number 4.2.2.2 Full crystallographic information is available from OCA.
Reference
The structure of Bacillus subtilis pectate lyase in complex with calcium., Pickersgill R, Jenkins J, Harris G, Nasser W, Robert-Baudouy J, Nat Struct Biol. 1994 Oct;1(10):717-23. PMID:7634076
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