1o71: Difference between revisions

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==Overview==

Sticholysin II (StnII) is a pore-forming protein (PFP) produced by the sea, anemone Stichodactyla helianthus. We found out that StnII exists in a, monomeric soluble state but forms tetramers in the presence of a lipidic, interface. Both structures have been independently determined at 1.7 A and, 18 A resolution, respectively, by using X-ray crystallography and electron, microscopy of two-dimensional crystals. Besides, the structure of soluble, StnII complexed with phosphocholine, determined at 2.4 A resolution, reveals a phospholipid headgroup binding site, which is located in a, region with an unusually high abundance of aromatic residues. Fitting of, the atomic model into the electron microscopy density envelope suggests, that while the beta sandwich structure of the protein remains intact upon, oligomerization, the N-terminal region and a flexible and highly basic, loop undergo significant conformational changes. These results provide the, structural basis for the membrane recognition step of actinoporins and, unexpected insights into the oligomerization step.

Sticholysin II (StnII) is a pore-forming protein (PFP) produced by the sea anemone Stichodactyla helianthus. We found out that StnII exists in a monomeric soluble state but forms tetramers in the presence of a lipidic interface. Both structures have been independently determined at 1.7 A and 18 A resolution, respectively, by using X-ray crystallography and electron microscopy of two-dimensional crystals. Besides, the structure of soluble StnII complexed with phosphocholine, determined at 2.4 A resolution, reveals a phospholipid headgroup binding site, which is located in a region with an unusually high abundance of aromatic residues. Fitting of the atomic model into the electron microscopy density envelope suggests that while the beta sandwich structure of the protein remains intact upon oligomerization, the N-terminal region and a flexible and highly basic loop undergo significant conformational changes. These results provide the structural basis for the membrane recognition step of actinoporins and unexpected insights into the oligomerization step.

==About this Structure==

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[[Category: Single protein]]

[[Category: Stichodactyla helianthus]]

[[Category: Gavilanes, J.G.]]

[[Category: Gavilanes, J G.]]

[[Category: Hermoso, J.A.]]

[[Category: Hermoso, J A.]]

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

[[Category: Mancheno, J M.]]

[[Category: Martinez-Ripoll, M.]]

[[Category: GOL]]

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[[Category: pore-forming toxin]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-Sticholysin II (StnII) is a pore-forming protein (PFP) produced by the sea, anemone Stichodactyla helianthus. We found out that StnII exists in a, monomeric soluble state but forms tetramers in the presence of a lipidic, interface. Both structures have been independently determined at 1.7 A and, 18 A resolution, respectively, by using X-ray crystallography and electron, microscopy of two-dimensional crystals. Besides, the structure of soluble, StnII complexed with phosphocholine, determined at 2.4 A resolution, reveals a phospholipid headgroup binding site, which is located in a, region with an unusually high abundance of aromatic residues. Fitting of, the atomic model into the electron microscopy density envelope suggests, that while the beta sandwich structure of the protein remains intact upon, oligomerization, the N-terminal region and a flexible and highly basic, loop undergo significant conformational changes. These results provide the, structural basis for the membrane recognition step of actinoporins and, unexpected insights into the oligomerization step.
+Sticholysin II (StnII) is a pore-forming protein (PFP) produced by the sea anemone Stichodactyla helianthus. We found out that StnII exists in a monomeric soluble state but forms tetramers in the presence of a lipidic interface. Both structures have been independently determined at 1.7 A and 18 A resolution, respectively, by using X-ray crystallography and electron microscopy of two-dimensional crystals. Besides, the structure of soluble StnII complexed with phosphocholine, determined at 2.4 A resolution, reveals a phospholipid headgroup binding site, which is located in a region with an unusually high abundance of aromatic residues. Fitting of the atomic model into the electron microscopy density envelope suggests that while the beta sandwich structure of the protein remains intact upon oligomerization, the N-terminal region and a flexible and highly basic loop undergo significant conformational changes. These results provide the structural basis for the membrane recognition step of actinoporins and unexpected insights into the oligomerization step.
 ==About this Structure==
@@ Line 13: / Line 13: @@
 [[Category: Single protein]]
 [[Category: Stichodactyla helianthus]]
-[[Category: Gavilanes, J.G.]]
+[[Category: Gavilanes, J G.]]
-[[Category: Hermoso, J.A.]]
+[[Category: Hermoso, J A.]]
-[[Category: Mancheno, J.M.]]
+[[Category: Mancheno, J M.]]
 [[Category: Martinez-Ripoll, M.]]
 [[Category: GOL]]
@@ Line 23: / Line 23: @@
 [[Category: pore-forming toxin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:54:18 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:14:05 2008''