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| - | [[Image:1zwx.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1zwx| PDB=1zwx | SCENE= }} | | {{STRUCTURE_1zwx| PDB=1zwx | SCENE= }} |
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| - | '''Crystal Structure of SmcL'''
| + | ===Crystal Structure of SmcL=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16093240}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16093240 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16093240}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Beta-hairpin]] | | [[Category: Beta-hairpin]] |
| | [[Category: Dnase1-like fold]] | | [[Category: Dnase1-like fold]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:10:43 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:06:42 2008'' |
Revision as of 08:06, 28 July 2008
Template:STRUCTURE 1zwx
Crystal Structure of SmcL
Template:ABSTRACT PUBMED 16093240
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
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