1ls1
From Proteopedia
(New page: 200px<br /><applet load="1ls1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ls1, resolution 1.10Å" /> '''T. aquaticus Ffh NG ...) |
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| - | [[Image:1ls1.gif|left|200px]]<br /><applet load="1ls1" size=" | + | [[Image:1ls1.gif|left|200px]]<br /><applet load="1ls1" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ls1, resolution 1.10Å" /> | caption="1ls1, resolution 1.10Å" /> | ||
'''T. aquaticus Ffh NG Domain at 1.1A Resolution'''<br /> | '''T. aquaticus Ffh NG Domain at 1.1A Resolution'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The NG domain of the prokaryotic signal recognition protein Ffh is a | + | The NG domain of the prokaryotic signal recognition protein Ffh is a two-domain GTPase that comprises part of the prokaryotic signal recognition particle (SRP) that functions in co-translational targeting of proteins to the membrane. The interface between the N and G domains includes two highly conserved sequence motifs and is adjacent in sequence and structure to one of the conserved GTPase signature motifs. Previous structural studies have shown that the relative orientation of the two domains is dynamic. The N domain of Ffh has been proposed to function in regulating the nucleotide-binding interactions of the G domain. However, biochemical studies suggest a more complex role for the domain in integrating communication between signal sequence recognition and interaction with receptor. Here, we report the structure of the apo NG GTPase of Ffh from Thermus aquaticus refined at 1.10 A resolution. Although the G domain is very well ordered in this structure, the N domain is less well ordered, reflecting the dynamic relationship between the two domains previously inferred. We demonstrate that the anisotropic displacement parameters directly visualize the underlying mobility between the two domains, and present a detailed structural analysis of the packing of the residues, including the critical alpha4 helix, that comprise the interface. Our data allows us to propose a structural explanation for the functional significance of sequence elements conserved at the N/G interface. |
==About this Structure== | ==About this Structure== | ||
| - | 1LS1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus] with MG and OXY as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1LS1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=OXY:'>OXY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LS1 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermus aquaticus]] | [[Category: Thermus aquaticus]] | ||
| - | [[Category: Freymann, D | + | [[Category: Freymann, D M.]] |
[[Category: Minasov, G.]] | [[Category: Minasov, G.]] | ||
| - | [[Category: Ramirez, U | + | [[Category: Ramirez, U D.]] |
[[Category: MG]] | [[Category: MG]] | ||
[[Category: OXY]] | [[Category: OXY]] | ||
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[[Category: ultrahigh resolution]] | [[Category: ultrahigh resolution]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:47:49 2008'' |
Revision as of 11:47, 21 February 2008
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T. aquaticus Ffh NG Domain at 1.1A Resolution
Overview
The NG domain of the prokaryotic signal recognition protein Ffh is a two-domain GTPase that comprises part of the prokaryotic signal recognition particle (SRP) that functions in co-translational targeting of proteins to the membrane. The interface between the N and G domains includes two highly conserved sequence motifs and is adjacent in sequence and structure to one of the conserved GTPase signature motifs. Previous structural studies have shown that the relative orientation of the two domains is dynamic. The N domain of Ffh has been proposed to function in regulating the nucleotide-binding interactions of the G domain. However, biochemical studies suggest a more complex role for the domain in integrating communication between signal sequence recognition and interaction with receptor. Here, we report the structure of the apo NG GTPase of Ffh from Thermus aquaticus refined at 1.10 A resolution. Although the G domain is very well ordered in this structure, the N domain is less well ordered, reflecting the dynamic relationship between the two domains previously inferred. We demonstrate that the anisotropic displacement parameters directly visualize the underlying mobility between the two domains, and present a detailed structural analysis of the packing of the residues, including the critical alpha4 helix, that comprise the interface. Our data allows us to propose a structural explanation for the functional significance of sequence elements conserved at the N/G interface.
About this Structure
1LS1 is a Single protein structure of sequence from Thermus aquaticus with and as ligands. Full crystallographic information is available from OCA.
Reference
Structural basis for mobility in the 1.1 A crystal structure of the NG domain of Thermus aquaticus Ffh., Ramirez UD, Minasov G, Focia PJ, Stroud RM, Walter P, Kuhn P, Freymann DM, J Mol Biol. 2002 Jul 19;320(4):783-99. PMID:12095255
Page seeded by OCA on Thu Feb 21 13:47:49 2008
Categories: Single protein | Thermus aquaticus | Freymann, D M. | Minasov, G. | Ramirez, U D. | MG | OXY | Ffh | Gtpase | Srp | Srp54 | Ultrahigh resolution
