1zug
From Proteopedia
(New page: 200px<br /><applet load="1zug" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zug" /> '''STRUCTURE OF PHAGE 434 CRO PROTEIN, NMR, 20 ...) |
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| - | [[Image:1zug.gif|left|200px]]<br /><applet load="1zug" size=" | + | [[Image:1zug.gif|left|200px]]<br /><applet load="1zug" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1zug" /> | caption="1zug" /> | ||
'''STRUCTURE OF PHAGE 434 CRO PROTEIN, NMR, 20 STRUCTURES'''<br /> | '''STRUCTURE OF PHAGE 434 CRO PROTEIN, NMR, 20 STRUCTURES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | 1H NMR resonances of the phage 434 Cro protein were assigned using | + | 1H NMR resonances of the phage 434 Cro protein were assigned using standard 2D NMR methods, and its solution structure determined using 867 distance constraints in distance geometry (DIANA) calculations ultimately refined by restrained molecular dynamics (GROMOS). In the 20 best NMR structures, the average pairwise backbone and heavy atom RMSDs are 0.63 +/- 0.14 and 1.53 +/- 0.15 A, respectively, for the structurally well-defined residues 4-65. Residues 1-3 and 66-71 at the N- and C-termini are structurally disordered. The region 4-65 includes five alpha-helices and tight turns which define the hydrophobic core of the protein. The backbone and heavy atom RMSDs for residues 4-65 are 0.92 +/- 0.12 and 1.99 +/- 0.12 A, respectively, for the NMR versus the crystal structures, but there are significant differences in the side-chain conformations and solvent accessibilities for some core residues. Analytical ultracentrifugation experiments confirm that 434 Cro is monomeric even at the high NMR concentrations. 434 Cro folding under NMR solution conditions is two-state as indicated by coincident urea denaturation curves from circular dichroism and intrinsic fluorescence measurements. They yield values for 434 Cro stability which show good correspondence to the free energy for global unfolding determined by NMR hydrogen exchange measurements for the slowest exchanging amide protons. |
==About this Structure== | ==About this Structure== | ||
| - | 1ZUG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_434 Bacteriophage 434]. Full crystallographic information is available from [http:// | + | 1ZUG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_434 Bacteriophage 434]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZUG OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Gimenez-Gallego, G.]] | [[Category: Gimenez-Gallego, G.]] | ||
[[Category: Gonzalez, C.]] | [[Category: Gonzalez, C.]] | ||
| - | [[Category: Jimenez, M | + | [[Category: Jimenez, M A.]] |
[[Category: Padmanabhan, S.]] | [[Category: Padmanabhan, S.]] | ||
[[Category: Rico, M.]] | [[Category: Rico, M.]] | ||
| - | [[Category: Sanz, J | + | [[Category: Sanz, J M.]] |
[[Category: gene regulating protein]] | [[Category: gene regulating protein]] | ||
[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:19:10 2008'' |
Revision as of 14:19, 21 February 2008
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STRUCTURE OF PHAGE 434 CRO PROTEIN, NMR, 20 STRUCTURES
Overview
1H NMR resonances of the phage 434 Cro protein were assigned using standard 2D NMR methods, and its solution structure determined using 867 distance constraints in distance geometry (DIANA) calculations ultimately refined by restrained molecular dynamics (GROMOS). In the 20 best NMR structures, the average pairwise backbone and heavy atom RMSDs are 0.63 +/- 0.14 and 1.53 +/- 0.15 A, respectively, for the structurally well-defined residues 4-65. Residues 1-3 and 66-71 at the N- and C-termini are structurally disordered. The region 4-65 includes five alpha-helices and tight turns which define the hydrophobic core of the protein. The backbone and heavy atom RMSDs for residues 4-65 are 0.92 +/- 0.12 and 1.99 +/- 0.12 A, respectively, for the NMR versus the crystal structures, but there are significant differences in the side-chain conformations and solvent accessibilities for some core residues. Analytical ultracentrifugation experiments confirm that 434 Cro is monomeric even at the high NMR concentrations. 434 Cro folding under NMR solution conditions is two-state as indicated by coincident urea denaturation curves from circular dichroism and intrinsic fluorescence measurements. They yield values for 434 Cro stability which show good correspondence to the free energy for global unfolding determined by NMR hydrogen exchange measurements for the slowest exchanging amide protons.
About this Structure
1ZUG is a Single protein structure of sequence from Bacteriophage 434. Full crystallographic information is available from OCA.
Reference
Three-dimensional solution structure and stability of phage 434 Cro protein., Padmanabhan S, Jimenez MA, Gonzalez C, Sanz JM, Gimenez-Gallego G, Rico M, Biochemistry. 1997 May 27;36(21):6424-36. PMID:9174359
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