1zwx: Difference between revisions

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[[Image:1zwx.gif|left|200px]]<br /><applet load="1zwx" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1zwx.gif|left|200px]]<br /><applet load="1zwx" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1zwx, resolution 1.900Å" />

'''Crystal Structure of SmcL'''<br />

==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.

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 [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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1ZWX OCA].

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==

Line 14:

[[Category: Single protein]]

[[Category: Sphingomyelin phosphodiesterase]]

[[Category: Banfield, M.J.]]

[[Category: Banfield, M J.]]

[[Category: Monzo, H.J.]]

[[Category: Monzo, H J.]]

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

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

[[Category: Race, P.R.]]

[[Category: Race, P R.]]

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

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

[[Category: GOL]]

[[Category: PO4]]

Line 24:

[[Category: dnase1-like fold]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:19:52 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1zwx.gif|left|200px]]<br /><applet load="1zwx" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1zwx.gif|left|200px]]<br /><applet load="1zwx" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1zwx, resolution 1.900&Aring;" />
 '''Crystal Structure of SmcL'''<br />
 ==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.
+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==
-ZWX 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZWX OCA].
+ZWX 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==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Sphingomyelin phosphodiesterase]]
-[[Category: Banfield, M.J.]]
+[[Category: Banfield, M J.]]
-[[Category: Monzo, H.J.]]
+[[Category: Monzo, H J.]]
-[[Category: Openshaw, A.E.A.]]
+[[Category: Openshaw, A E.A.]]
-[[Category: Race, P.R.]]
+[[Category: Race, P R.]]
-[[Category: Vasquez-Boland, J.A.]]
+[[Category: Vasquez-Boland, J A.]]
 [[Category: GOL]]
 [[Category: PO4]]
@@ Line 24: / Line 24: @@
 [[Category: dnase1-like fold]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:42:46 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:19:52 2008''