1zwx

<table><tr><td colspan='2'>[[1zwx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"listeria_bulgarica"_ivanov_1975 "listeria bulgarica" ivanov 1975]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZWX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZWX FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">smcl ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1638 "Listeria bulgarica" Ivanov 1975])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Sphingomyelin_phosphodiesterase Sphingomyelin phosphodiesterase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.12 3.1.4.12] </span></td></tr>

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

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.

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<ref>PMID:16093240</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 1zwx" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Listeria bulgarica ivanov 1975]]

[[Category: Sphingomyelin phosphodiesterase]]

[[Category: Banfield, M J]]

[[Category: Monzo, H J]]

[[Category: Openshaw, A E.A]]

[[Category: Race, P R]]

[[Category: Vasquez-Boland, J A]]

[[Category: Hydrolase]]