2a2y
From Proteopedia
(New page: 200px<br /><applet load="2a2y" size="450" color="white" frame="true" align="right" spinBox="true" caption="2a2y" /> '''NMR Structue of Sso10b2 from Sulfolobus solf...) |
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| - | [[Image:2a2y.gif|left|200px]]<br /><applet load="2a2y" size=" | + | [[Image:2a2y.gif|left|200px]]<br /><applet load="2a2y" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''NMR Structue of Sso10b2 from Sulfolobus solfataricus'''<br /> | '''NMR Structue of Sso10b2 from Sulfolobus solfataricus'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The Sso10b (or Alba) family of proteins is a conserved group of archaeal | + | The Sso10b (or Alba) family of proteins is a conserved group of archaeal and eukaryotic proteins which are thought to play a role in both chromatin organization and RNA metabolism. We describe here the solution structure and properties of Sso10b2 from Sulfolobus solfataricus. NMR data including residual dipolar couplings and (15)N relaxation data demonstrated that the protein adopts a beta(1)alpha(1)beta(2)alpha(2)beta(3)beta(4) topology with an IF-3-like fold. The protein dimerizes in solution at 30 degrees C via a hydrophobic surface defined by the C-terminal alpha(2)beta(3)beta(4) elements with a structure similar to one of the putative dimers indicated by previous crystal structures. DSC and circular dichroism data demonstrated an unusual two-state structural transition near the growth temperature which led to an increase in beta-sheet content without dissociation of the dimer. The cooperativity of the transition exceeded that of a dimer at pH 7, demonstrating the presence of higher order oligomers near the growth temperature at pH 7. Reverse titrations of Sso10b2 with nucleic acid showed that the protein binds single-stranded DNA (K(d) of 3 x 10(-)(7) M) with higher affinity than RNA (1.3 x 10(-)(6) M) or double-stranded DNA (1.5 x 10(-)(5) M) in 10 mM KH(2)PO(4) (pH 7.0, 20 degrees C). NMR chemical shift perturbation data indicated that single-stranded DNA and RNA binding occurred across the same dimer interface and encompassed a surface defined by the C-terminal ends of the beta(1), beta(2), and beta(3) strands of each monomer. |
==About this Structure== | ==About this Structure== | ||
| - | 2A2Y is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus]. Full crystallographic information is available from [http:// | + | 2A2Y is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A2Y OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Sulfolobus solfataricus]] | [[Category: Sulfolobus solfataricus]] | ||
| - | [[Category: Armstrong, T | + | [[Category: Armstrong, T L.]] |
[[Category: Biyani, K.]] | [[Category: Biyani, K.]] | ||
| - | [[Category: Clark, A | + | [[Category: Clark, A T.]] |
| - | [[Category: Edmondson, S | + | [[Category: Edmondson, S P.]] |
| - | [[Category: Kahsai, M | + | [[Category: Kahsai, M A.]] |
| - | [[Category: Shriver, J | + | [[Category: Shriver, J W.]] |
[[Category: dimer]] | [[Category: dimer]] | ||
[[Category: hyperthermophile protein]] | [[Category: hyperthermophile protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:23:08 2008'' |
Revision as of 14:23, 21 February 2008
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NMR Structue of Sso10b2 from Sulfolobus solfataricus
Overview
The Sso10b (or Alba) family of proteins is a conserved group of archaeal and eukaryotic proteins which are thought to play a role in both chromatin organization and RNA metabolism. We describe here the solution structure and properties of Sso10b2 from Sulfolobus solfataricus. NMR data including residual dipolar couplings and (15)N relaxation data demonstrated that the protein adopts a beta(1)alpha(1)beta(2)alpha(2)beta(3)beta(4) topology with an IF-3-like fold. The protein dimerizes in solution at 30 degrees C via a hydrophobic surface defined by the C-terminal alpha(2)beta(3)beta(4) elements with a structure similar to one of the putative dimers indicated by previous crystal structures. DSC and circular dichroism data demonstrated an unusual two-state structural transition near the growth temperature which led to an increase in beta-sheet content without dissociation of the dimer. The cooperativity of the transition exceeded that of a dimer at pH 7, demonstrating the presence of higher order oligomers near the growth temperature at pH 7. Reverse titrations of Sso10b2 with nucleic acid showed that the protein binds single-stranded DNA (K(d) of 3 x 10(-)(7) M) with higher affinity than RNA (1.3 x 10(-)(6) M) or double-stranded DNA (1.5 x 10(-)(5) M) in 10 mM KH(2)PO(4) (pH 7.0, 20 degrees C). NMR chemical shift perturbation data indicated that single-stranded DNA and RNA binding occurred across the same dimer interface and encompassed a surface defined by the C-terminal ends of the beta(1), beta(2), and beta(3) strands of each monomer.
About this Structure
2A2Y is a Single protein structure of sequence from Sulfolobus solfataricus. Full crystallographic information is available from OCA.
Reference
Solution structure, stability, and nucleic acid binding of the hyperthermophile protein Sso10b2., Biyani K, Kahsai MA, Clark AT, Armstrong TL, Edmondson SP, Shriver JW, Biochemistry. 2005 Nov 1;44(43):14217-30. PMID:16245938
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