1zwx

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[[Image:1zwx.gif|left|200px]]
[[Image:1zwx.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1zwx |SIZE=350|CAPTION= <scene name='initialview01'>1zwx</scene>, resolution 1.900&Aring;
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The line below this paragraph, containing "STRUCTURE_1zwx", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Sphingomyelin_phosphodiesterase Sphingomyelin phosphodiesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.12 3.1.4.12] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= smcl ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1638 Listeria ivanovii])
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-->
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|DOMAIN=
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{{STRUCTURE_1zwx| PDB=1zwx | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zwx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zwx OCA], [http://www.ebi.ac.uk/pdbsum/1zwx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zwx RCSB]</span>
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}}
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'''Crystal Structure of SmcL'''
'''Crystal Structure of SmcL'''
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[[Category: Race, P R.]]
[[Category: Race, P R.]]
[[Category: Vasquez-Boland, J A.]]
[[Category: Vasquez-Boland, J A.]]
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[[Category: beta-hairpin]]
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[[Category: Beta-hairpin]]
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[[Category: dnase1-like fold]]
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[[Category: Dnase1-like fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:10:43 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:42:43 2008''
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Revision as of 15:10, 3 May 2008

Image:1zwx.gif

Template:STRUCTURE 1zwx

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. 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 Page seeded by OCA on Sat May 3 18:10:43 2008

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