2oj6
From Proteopedia
(New page: 200px<br /><applet load="2oj6" size="350" color="white" frame="true" align="right" spinBox="true" caption="2oj6, resolution 1.85Å" /> '''Crystal Structure of...) |
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==Overview== | ==Overview== | ||
| - | Reovirus attachment protein sigma1 mediates engagement of receptors on the | + | Reovirus attachment protein sigma1 mediates engagement of receptors on the surface of target cells and undergoes dramatic conformational rearrangements during viral disassembly in the endocytic pathway. The sigma1 protein is a filamentous, trimeric molecule with a globular beta-barrel head domain. An unusual cluster of aspartic acid residues sandwiched between hydrophobic tyrosines is located at the sigma1 subunit interface. A 1.75-A structure of the sigma1 head domain now reveals two water molecules at the subunit interface that are held strictly in position and interact with neighboring residues. Structural and biochemical analyses of mutants affecting the aspartic acid sandwich indicate that these residues and the corresponding chelated water molecules act as a plug to block the free flow of solvent and stabilize the trimer. This arrangement of residues at the sigma1 head trimer interface illustrates a new protein design motif that may confer conformational mobility during cell entry. |
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | The | + | The reovirus sigma1 aspartic acid sandwich: a trimerization motif poised for conformational change., Schelling P, Guglielmi KM, Kirchner E, Paetzold B, Dermody TS, Stehle T, J Biol Chem. 2007 Apr 13;282(15):11582-9. Epub 2007 Feb 15. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17303562 17303562] |
[[Category: Reovirus sp.]] | [[Category: Reovirus sp.]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Dermody, T | + | [[Category: Dermody, T S.]] |
[[Category: Kirchner, E.]] | [[Category: Kirchner, E.]] | ||
[[Category: Stehle, T.]] | [[Category: Stehle, T.]] | ||
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[[Category: trimer]] | [[Category: trimer]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:19:04 2008'' |
Revision as of 16:19, 21 February 2008
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Crystal Structure of Reovirus T3D Attachment Protein Sigma1 head domain D345N mutant
Overview
Reovirus attachment protein sigma1 mediates engagement of receptors on the surface of target cells and undergoes dramatic conformational rearrangements during viral disassembly in the endocytic pathway. The sigma1 protein is a filamentous, trimeric molecule with a globular beta-barrel head domain. An unusual cluster of aspartic acid residues sandwiched between hydrophobic tyrosines is located at the sigma1 subunit interface. A 1.75-A structure of the sigma1 head domain now reveals two water molecules at the subunit interface that are held strictly in position and interact with neighboring residues. Structural and biochemical analyses of mutants affecting the aspartic acid sandwich indicate that these residues and the corresponding chelated water molecules act as a plug to block the free flow of solvent and stabilize the trimer. This arrangement of residues at the sigma1 head trimer interface illustrates a new protein design motif that may confer conformational mobility during cell entry.
About this Structure
2OJ6 is a Single protein structure of sequence from Reovirus sp. with as ligand. Full crystallographic information is available from OCA.
Reference
The reovirus sigma1 aspartic acid sandwich: a trimerization motif poised for conformational change., Schelling P, Guglielmi KM, Kirchner E, Paetzold B, Dermody TS, Stehle T, J Biol Chem. 2007 Apr 13;282(15):11582-9. Epub 2007 Feb 15. PMID:17303562
Page seeded by OCA on Thu Feb 21 18:19:04 2008
