1zwx
From Proteopedia
(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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| - | [[Image:1zwx.gif|left|200px]]<br /><applet load="1zwx" size=" | + | [[Image:1zwx.gif|left|200px]]<br /><applet load="1zwx" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1zwx, resolution 1.900Å" /> | caption="1zwx, resolution 1.900Å" /> | ||
'''Crystal Structure of SmcL'''<br /> | '''Crystal Structure of SmcL'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Sphingomyelinases C are enzymes that catalyze the hydrolysis of | + | 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== | ==About this Structure== | ||
| - | 1ZWX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Listeria_ivanovii Listeria ivanovii] with PO4 and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 1ZWX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Listeria_ivanovii Listeria ivanovii] with <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZWX OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Sphingomyelin phosphodiesterase]] | [[Category: Sphingomyelin phosphodiesterase]] | ||
| - | [[Category: Banfield, M | + | [[Category: Banfield, M J.]] |
| - | [[Category: Monzo, H | + | [[Category: Monzo, H J.]] |
| - | [[Category: Openshaw, A | + | [[Category: Openshaw, A E.A.]] |
| - | [[Category: Race, P | + | [[Category: Race, P R.]] |
| - | [[Category: Vasquez-Boland, J | + | [[Category: Vasquez-Boland, J A.]] |
[[Category: GOL]] | [[Category: GOL]] | ||
[[Category: PO4]] | [[Category: PO4]] | ||
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[[Category: dnase1-like fold]] | [[Category: dnase1-like fold]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:19:52 2008'' |
Revision as of 14:19, 21 February 2008
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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 and 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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