1x36
From Proteopedia
(New page: 200px<br /><applet load="1x36" size="450" color="white" frame="true" align="right" spinBox="true" caption="1x36, resolution 2.70Å" /> '''T=1 capsid of an ami...) |
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| - | [[Image:1x36.gif|left|200px]]<br /><applet load="1x36" size=" | + | [[Image:1x36.gif|left|200px]]<br /><applet load="1x36" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1x36, resolution 2.70Å" /> | caption="1x36, resolution 2.70Å" /> | ||
'''T=1 capsid of an amino-terminal deletion mutant of SeMV CP'''<br /> | '''T=1 capsid of an amino-terminal deletion mutant of SeMV CP'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Deletion of the N-terminal 31 amino acids from the coat protein (CP) of | + | Deletion of the N-terminal 31 amino acids from the coat protein (CP) of Sesbania mosaic virus (SeMV) results in the formation of T = 1 capsids. The X-ray crystal structure of CP-NDelta31 mutant capsids reveals that the CP adopts a conformation similar to those of other T = 1 mutants. The 40 N-terminal residues are disordered in CP-NDelta31. The intersubunit hydrogen bonds closely resemble those of the native capsid. The role of water molecules in the SeMV structure has been analyzed for the first time using the present structure. As many as 139 of the 173 waters per subunit make direct contacts with the protein atoms. The water molecules form a robust scaffold around the capsid, stabilize the loops and provide integrity to the subunit. These waters constitute a network connecting diametrically opposite ends of the subunit. Such waters might act as nodes for conveying signals for assembly or disassembly across a large conformational space. Many water-mediated interactions are observed at various interfaces. The twofold interface, which has the smallest number of protein-protein contacts, is primarily held by water-mediated interactions. The present structure illuminates the role of water molecules in the structure and stability of the capsid and points out their possible significance in assembly. |
==About this Structure== | ==About this Structure== | ||
| - | 1X36 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sesbania_mosaic_virus Sesbania mosaic virus] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1X36 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sesbania_mosaic_virus Sesbania mosaic virus] 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=1X36 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Sesbania mosaic virus]] | [[Category: Sesbania mosaic virus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Murthy, M | + | [[Category: Murthy, M R.]] |
[[Category: Sangita, V.]] | [[Category: Sangita, V.]] | ||
| - | [[Category: Satheshkumar, P | + | [[Category: Satheshkumar, P S.]] |
| - | [[Category: Savithri, H | + | [[Category: Savithri, H S.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: icosahedral virus]] | [[Category: icosahedral virus]] | ||
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[[Category: t=1 capsid]] | [[Category: t=1 capsid]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:50:37 2008'' |
Revision as of 13:50, 21 February 2008
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T=1 capsid of an amino-terminal deletion mutant of SeMV CP
Overview
Deletion of the N-terminal 31 amino acids from the coat protein (CP) of Sesbania mosaic virus (SeMV) results in the formation of T = 1 capsids. The X-ray crystal structure of CP-NDelta31 mutant capsids reveals that the CP adopts a conformation similar to those of other T = 1 mutants. The 40 N-terminal residues are disordered in CP-NDelta31. The intersubunit hydrogen bonds closely resemble those of the native capsid. The role of water molecules in the SeMV structure has been analyzed for the first time using the present structure. As many as 139 of the 173 waters per subunit make direct contacts with the protein atoms. The water molecules form a robust scaffold around the capsid, stabilize the loops and provide integrity to the subunit. These waters constitute a network connecting diametrically opposite ends of the subunit. Such waters might act as nodes for conveying signals for assembly or disassembly across a large conformational space. Many water-mediated interactions are observed at various interfaces. The twofold interface, which has the smallest number of protein-protein contacts, is primarily held by water-mediated interactions. The present structure illuminates the role of water molecules in the structure and stability of the capsid and points out their possible significance in assembly.
About this Structure
1X36 is a Single protein structure of sequence from Sesbania mosaic virus with as ligand. Full crystallographic information is available from OCA.
Reference
Structure of a mutant T=1 capsid of Sesbania mosaic virus: role of water molecules in capsid architecture and integrity., Sangita V, Satheshkumar PS, Savithri HS, Murthy MR, Acta Crystallogr D Biol Crystallogr. 2005 Oct;61(Pt 10):1406-12. Epub 2005, Sep 28. PMID:16204894
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