1aei: Difference between revisions

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New page: left|200px<br /><applet load="1aei" size="450" color="white" frame="true" align="right" spinBox="true" caption="1aei, resolution 2.8Å" /> '''CRYSTAL STRUCTURE OF ...
 
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[[Image:1aei.jpg|left|200px]]<br /><applet load="1aei" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1aei.jpg|left|200px]]<br /><applet load="1aei" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1aei, resolution 2.8&Aring;" />
caption="1aei, resolution 2.8&Aring;" />
'''CRYSTAL STRUCTURE OF THE ANNEXIN XII HEXAMER'''<br />
'''CRYSTAL STRUCTURE OF THE ANNEXIN XII HEXAMER'''<br />


==Overview==
==Overview==
Annexins are a family of calcium- and phospholipid-binding proteins, implicated in a number of biological processes including membrane fusion, and ion channel formation. The crystal structure of the annexin XII, hexamer, refined at 2.8 A resolution, forms a concave disk with 3-2, symmetry, about 100 A in diameter and 70 A thick with a central, hydrophilic pore. Six intermolecular Ca2+ ions are involved in hexamer, formation. An additional 18 Ca2+ ions are located on the perimeter of the, disk, accessible only from the side of the hexameric disk. On the basis of, the hexamer structure we propose here a new mode of protein-phospholipid, bilayer interaction that is distinct from the hydrophobic insertion of, typical membrane proteins. This speculative model postulates the, Ca(2+)-dependent insertion of the hydrophilic annexin XII hexamer into, phospholipid bilayers with local reorientation of the bilayer, phospholipids.
Annexins are a family of calcium- and phospholipid-binding proteins implicated in a number of biological processes including membrane fusion and ion channel formation. The crystal structure of the annexin XII hexamer, refined at 2.8 A resolution, forms a concave disk with 3-2 symmetry, about 100 A in diameter and 70 A thick with a central hydrophilic pore. Six intermolecular Ca2+ ions are involved in hexamer formation. An additional 18 Ca2+ ions are located on the perimeter of the disk, accessible only from the side of the hexameric disk. On the basis of the hexamer structure we propose here a new mode of protein-phospholipid bilayer interaction that is distinct from the hydrophobic insertion of typical membrane proteins. This speculative model postulates the Ca(2+)-dependent insertion of the hydrophilic annexin XII hexamer into phospholipid bilayers with local reorientation of the bilayer phospholipids.


==About this Structure==
==About this Structure==
1AEI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hydra_vulgaris Hydra vulgaris] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AEI OCA].  
1AEI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hydra_vulgaris Hydra vulgaris] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AEI OCA].  


==Reference==
==Reference==
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[[Category: Hydra vulgaris]]
[[Category: Hydra vulgaris]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Chang, B.T.]]
[[Category: Chang, B T.]]
[[Category: Haigler, H.T.]]
[[Category: Haigler, H T.]]
[[Category: Luecke, H.]]
[[Category: Luecke, H.]]
[[Category: Mailliard, W.S.]]
[[Category: Mailliard, W S.]]
[[Category: Schlaepfer, D.D.]]
[[Category: Schlaepfer, D D.]]
[[Category: CA]]
[[Category: CA]]
[[Category: annexin]]
[[Category: annexin]]
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[[Category: phospholipid]]
[[Category: phospholipid]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:47:43 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:43:37 2008''

Revision as of 12:43, 21 February 2008

File:1aei.jpg


1aei, resolution 2.8Å

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CRYSTAL STRUCTURE OF THE ANNEXIN XII HEXAMER

OverviewOverview

Annexins are a family of calcium- and phospholipid-binding proteins implicated in a number of biological processes including membrane fusion and ion channel formation. The crystal structure of the annexin XII hexamer, refined at 2.8 A resolution, forms a concave disk with 3-2 symmetry, about 100 A in diameter and 70 A thick with a central hydrophilic pore. Six intermolecular Ca2+ ions are involved in hexamer formation. An additional 18 Ca2+ ions are located on the perimeter of the disk, accessible only from the side of the hexameric disk. On the basis of the hexamer structure we propose here a new mode of protein-phospholipid bilayer interaction that is distinct from the hydrophobic insertion of typical membrane proteins. This speculative model postulates the Ca(2+)-dependent insertion of the hydrophilic annexin XII hexamer into phospholipid bilayers with local reorientation of the bilayer phospholipids.

About this StructureAbout this Structure

1AEI is a Single protein structure of sequence from Hydra vulgaris with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the annexin XII hexamer and implications for bilayer insertion., Luecke H, Chang BT, Mailliard WS, Schlaepfer DD, Haigler HT, Nature. 1995 Nov 30;378(6556):512-5. PMID:7477411

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