1zwx
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(New page: 200px<br /><applet load="1zwx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zwx, resolution 1.900Å" /> '''Crystal Structure o...)
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Revision as of 05:35, 21 November 2007
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Crystal Structure of SmcL
Overview
Sphingomyelinases C are enzymes that catalyze the hydrolysis of, sphingomyelin in biological membranes to ceramide and phosphorylcholine., Various pathogenic bacteria produce secreted neutral sphingomyelinases C, that act as membrane-damaging virulence factors. Mammalian neutral, sphingomyelinases C, which display sequence homology to the bacterial, enzymes, are involved in sphingolipid metabolism and signaling. This, article describes the first structure to be determined for a member of the, neutral sphingomyelinase C family, SmcL, from the intracellular bacterial, pathogen Listeria ivanovii. The structure has been refined to 1.9-A, resolution with phases derived by single isomorphous replacement with, anomalous scattering techniques from a single iridium derivative. SmcL, adopts a DNase I-like fold, and is the first member of this protein, superfamily to have its structure determined that acts as a phospholipase., The structure reveals several unique features that adapt the protein to, its phospholipid substrate. These include large hydrophobic beta-hairpin, and hydrophobic loops surrounding the active site that may bind and, penetrate the lipid bilayer to position sphingomyelin in a catalytically, competent position. The structure also provides insight into the proposed, general base/acid catalytic mechanism, in which His-325 and His-185 play, key roles.
About this Structure
1ZWX is a Single protein structure of sequence from Listeria ivanovii with PO4 and GOL as ligands. Active as Sphingomyelin phosphodiesterase, with EC number 3.1.4.12 Full crystallographic information is available from OCA.
Reference
Crystal structure of SmcL, a bacterial neutral sphingomyelinase C from Listeria., Openshaw AE, Race PR, Monzo HJ, Vazquez-Boland JA, Banfield MJ, J Biol Chem. 2005 Oct 14;280(41):35011-7. Epub 2005 Aug 10. PMID:16093240
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