1plu
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(New page: 200px<br /><applet load="1plu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1plu, resolution 2.2Å" /> '''PECTATE LYASE C FROM ...)
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Revision as of 21:47, 20 November 2007
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PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI WITH 1 LU+3 ION IN THE PUTATIVE CALCIUM BINDING SITE
Overview
The crystal structure of pectate lyase C (EC 4.2.2.2) from the, enterobacterium Erwinia chrysanthemi (PelC) has been refined by molecular, dynamics techniques to a resolution of 2.2 A to an R factor of 17.97%. The, final model consists of 352 of the total 353 amino acids and 114 solvent, molecules. The root-mean-square deviation from ideality is 0.009 A for, bond lengths and 1.768[deg] for bond angles. The structure of PelC bound, to the lanthanide ion lutetium, used as a calcium analog, has also been, refined. Lutetium inhibits the enzymatic activity of the protein, and in, the PelC-lutetium structure, the ion binds in the putative calcium-binding, site. Five side-chain atoms form ligands to the lutetium ion. An analysis, of the atomic-level model of the two protein structures reveals possible, implications for the enzymatic mechanism of the enzyme.
About this Structure
1PLU is a Single protein structure of sequence from Erwinia chrysanthemi with LU as ligand. Active as Pectate lyase, with EC number 4.2.2.2 Full crystallographic information is available from OCA.
Reference
The Refined Three-Dimensional Structure of Pectate Lyase C from Erwinia chrysanthemi at 2.2 Angstrom Resolution (Implications for an Enzymatic Mechanism)., Yoder MD, Jurnak F, Plant Physiol. 1995 Feb;107(2):349-364. PMID:12228363
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