1o8h
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(New page: 200px<br /> <applet load="1o8h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1o8h, resolution 2.20Å" /> '''PECTATE LYASE C FRO...)
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Revision as of 17:13, 29 October 2007
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PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI AT PH 9.5 WITH 0.3MM CA2+ ADDED
Overview
Ca(2+) is essential for in vitro activity of Erwinia chrysanthemi pectate, lyase C (PelC). Crystallographic analyses of 11 PelC-Ca(2+) complexes, formed at pH 4.5, 9.5, and 11.2 under varying Ca(2+) concentrations, have, been solved and refined at a resolution of 2.2 A. The Ca(2+) site, represents a new motif for Ca(2+), consisting primarily of beta-turns and, beta-strands. The principal differences between PelC and the PelC-Ca(2+), structures at all pH values are the side-chain conformations of Asp-129, and Glu-166 as well as the occupancies of four water molecules. According, to calculations of pK(a) values, the presence of Ca(2+) and associated, structural changes lower the pK(a) of Arg-218, the amino acid responsible, for proton abstraction during catalysis. The Ca(2+) affinity for ... [(full description)]
About this Structure
1O8H is a [Single protein] structure of sequence from [Erwinia chrysanthemi] with CA as [ligand]. Active as [[1]], with EC number [4.2.2.2]. Full crystallographic information is available from [OCA].
Reference
Characterization and implications of Ca2+ binding to pectate lyase C., Herron SR, Scavetta RD, Garrett M, Legner M, Jurnak F, J Biol Chem. 2003 Apr 4;278(14):12271-7. Epub 2003 Jan 22. PMID:12540845
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