2z8l: Difference between revisions

Revision as of 20:00, 21 February 2008

Crystal Structure of the Staphylococcal superantigen-like protein SSL5 at pH 4.6 complexed with sialyl Lewis X

OverviewOverview

Staphylococcus aureus is a significant human pathogen. Among its large repertoire of secreted toxins is a group of staphylococcal superantigen-like proteins (SSLs). These are homologous to superantigens but do not have the same activity. SSL5 is shown here to bind to human granulocytes and to the cell surface receptors for human IgA (Fc alphaRI) and P-selectin [P-selectin glycoprotein ligand-1 (PSGL-1)] in a sialic acid (Sia)-dependent manner. Co-crystallization of SSL5 with the tetrasaccharide sialyl Lewis X (sLe(X)), a key determinant of PSGL-1 binding to P-selectin, led to crystal structures of the SSL5-sLe(X) complex at resolutions of 1.65 and 2.75 A for crystals at two pH values. In both structures, sLe(X) bound to a specific site on the surface of the C-terminal domain of SSL5 in a conformation identical with that bound by P-selectin. Conservation of the key carbohydrate binding residues indicates that this ability to bind human glycans is shared by a substantial subgroup of the SSLs, including SSL2, SSL3, SSL4, SSL5, SSL6, and SSL11. This indicates that the ability to target human glycans is an important property of this group of toxins. Structural comparisons also showed that the Sia binding site in SSL5 contains a substructure that is shared by other Sia binding proteins from bacteria as well as viruses and represents a common binding motif.

About this StructureAbout this Structure

2Z8L is a Single protein structure of sequence from Staphylococcus aureus with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structures of the staphylococcal toxin SSL5 in complex with sialyl Lewis X reveal a conserved binding site that shares common features with viral and bacterial sialic acid binding proteins., Baker HM, Basu I, Chung MC, Caradoc-Davies T, Fraser JD, Baker EN, J Mol Biol. 2007 Dec 14;374(5):1298-308. Epub 2007 Oct 10. PMID:17996251

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 ==Overview==
-Staphylococcus aureus is a significant human pathogen. Among its large, repertoire of secreted toxins is a group of staphylococcal, superantigen-like proteins (SSLs). These are homologous to superantigens, but do not have the same activity. SSL5 is shown here to bind to human, granulocytes and to the cell surface receptors for human IgA (Fc alphaRI), and P-selectin [P-selectin glycoprotein ligand-1 (PSGL-1)] in a sialic, acid (Sia)-dependent manner. Co-crystallization of SSL5 with the, tetrasaccharide sialyl Lewis X (sLe(X)), a key determinant of PSGL-1, binding to P-selectin, led to crystal structures of the SSL5-sLe(X), complex at resolutions of 1.65 and 2.75 A for crystals at two pH values., In both structures, sLe(X) bound to a specific site on the surface of the, C-terminal domain of SSL5 in a conformation identical with that bound by, P-selectin. Conservation of the key carbohydrate binding residues, indicates that this ability to bind human glycans is shared by a, substantial subgroup of the SSLs, including SSL2, SSL3, SSL4, SSL5, SSL6, and SSL11. This indicates that the ability to target human glycans is an, important property of this group of toxins. Structural comparisons also, showed that the Sia binding site in SSL5 contains a substructure that is, shared by other Sia binding proteins from bacteria as well as viruses and, represents a common binding motif.
+Staphylococcus aureus is a significant human pathogen. Among its large repertoire of secreted toxins is a group of staphylococcal superantigen-like proteins (SSLs). These are homologous to superantigens but do not have the same activity. SSL5 is shown here to bind to human granulocytes and to the cell surface receptors for human IgA (Fc alphaRI) and P-selectin [P-selectin glycoprotein ligand-1 (PSGL-1)] in a sialic acid (Sia)-dependent manner. Co-crystallization of SSL5 with the tetrasaccharide sialyl Lewis X (sLe(X)), a key determinant of PSGL-1 binding to P-selectin, led to crystal structures of the SSL5-sLe(X) complex at resolutions of 1.65 and 2.75 A for crystals at two pH values. In both structures, sLe(X) bound to a specific site on the surface of the C-terminal domain of SSL5 in a conformation identical with that bound by P-selectin. Conservation of the key carbohydrate binding residues indicates that this ability to bind human glycans is shared by a substantial subgroup of the SSLs, including SSL2, SSL3, SSL4, SSL5, SSL6, and SSL11. This indicates that the ability to target human glycans is an important property of this group of toxins. Structural comparisons also showed that the Sia binding site in SSL5 contains a substructure that is shared by other Sia binding proteins from bacteria as well as viruses and represents a common binding motif.
 ==About this Structure==
@@ Line 13: / Line 13: @@
 [[Category: Single protein]]
 [[Category: Staphylococcus aureus]]
-[[Category: Baker, E.N.]]
+[[Category: Baker, E N.]]
-[[Category: Baker, H.M.]]
+[[Category: Baker, H M.]]
 [[Category: Basu, I.]]
-[[Category: Chung, M.C.]]
+[[Category: Chung, M C.]]
-[[Category: Davies, T.Caradoc.]]
+[[Category: Davies, T Caradoc.]]
-[[Category: Fraser, J.D.]]
+[[Category: Fraser, J D.]]
 [[Category: GOL]]
 [[Category: PO4]]
@@ Line 25: / Line 25: @@
 [[Category: sugar binding protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:41:33 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:00:47 2008''