1ftz: Difference between revisions

Revision as of 13:42, 21 February 2008

NUCLEAR MAGNETIC RESONANCE SOLUTION STRUCTURE OF THE FUSHI TARAZU HOMEODOMAIN FROM DROSOPHILA AND COMPARISON WITH THE ANTENNAPEDIA HOMEODOMAIN

OverviewOverview

The three-dimensional structure of a recombinant 70-residue polypeptide containing the complete fushi tarazu (ftz) homeodomain from Drosophila melanogaster has been determined by nuclear magnetic resonance (NMR) spectroscopy in solution. On the basis of 915 upper distance constraints derived from nuclear Overhauser effects and 178 dihedral angle constraints, a group of 20 conformers representing the solution structure of the ftz homeodomain was computed with the program DIANA and energy-minimized with the program OPAL. The average of the pairwise root-mean-square deviations of the individual NMR conformers relative to the mean coordinates is 0.50 A for the backbone atoms N, C alpha and C' of residues 8 to 53. The molecular architecture includes three helices comprising the residues 10 to 21, 28 to 38, and 42 to 52, a loop of residues 22 to 27 between the helices I and II, and a turn of residues 39 to 41 linking the helices II and III. Comparisons with the structure of the mutant Antennapedia homeodomain with Cys39 replaced by Ser, Antp (C39S), shows that the two proteins contain the same molecular fold for residues 8 to 53, whereas the more flexible fourth helix comprising residues 53 to 59 in the Antp (C39S) homeodomain has no counterpart in the ftz homeodomain. Considering that important intermolecular interactions in the DNA complexes with the Antp, engrailed and Mat alpha 2 homeodomains involve the fourth helix, it was rather unexpected that the stability of the complex of ftz with the BS2 operator site was found to be comparable to or even somewhat higher than that of the Antp complex with BS2. Another difference is that the Antp homeodomain is more stable with respect to thermal denaturation, with denaturation temperatures at pH 4.8 of 27 degrees C and 48 degrees C, respectively, for ftz and Antp.

About this StructureAbout this Structure

1FTZ is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.

ReferenceReference

Nuclear magnetic resonance solution structure of the fushi tarazu homeodomain from Drosophila and comparison with the Antennapedia homeodomain., Qian YQ, Furukubo-Tokunaga K, Resendez-Perez D, Muller M, Gehring WJ, Wuthrich K, J Mol Biol. 1994 May 6;238(3):333-45. PMID:7909851

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OCA

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-[[Image:1ftz.gif|left|200px]]<br /><applet load="1ftz" size="450" color="white" frame="true" align="right" spinBox="true"
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 caption="1ftz" />
 '''NUCLEAR MAGNETIC RESONANCE SOLUTION STRUCTURE OF THE FUSHI TARAZU HOMEODOMAIN FROM DROSOPHILA AND COMPARISON WITH THE ANTENNAPEDIA HOMEODOMAIN'''<br />
 ==Overview==
-The three-dimensional structure of a recombinant 70-residue polypeptide, containing the complete fushi tarazu (ftz) homeodomain from Drosophila, melanogaster has been determined by nuclear magnetic resonance (NMR), spectroscopy in solution. On the basis of 915 upper distance constraints, derived from nuclear Overhauser effects and 178 dihedral angle, constraints, a group of 20 conformers representing the solution structure, of the ftz homeodomain was computed with the program DIANA and, energy-minimized with the program OPAL. The average of the pairwise, root-mean-square deviations of the individual NMR conformers relative to, the mean coordinates is 0.50 A for the backbone atoms N, C alpha and C' of, residues 8 to 53. The molecular architecture includes three helices, comprising the residues 10 to 21, 28 to 38, and 42 to 52, a loop of, residues 22 to 27 between the helices I and II, and a turn of residues 39, to 41 linking the helices II and III. Comparisons with the structure of, the mutant Antennapedia homeodomain with Cys39 replaced by Ser, Antp, (C39S), shows that the two proteins contain the same molecular fold for, residues 8 to 53, whereas the more flexible fourth helix comprising, residues 53 to 59 in the Antp (C39S) homeodomain has no counterpart in the, ftz homeodomain. Considering that important intermolecular interactions in, the DNA complexes with the Antp, engrailed and Mat alpha 2 homeodomains, involve the fourth helix, it was rather unexpected that the stability of, the complex of ftz with the BS2 operator site was found to be comparable, to or even somewhat higher than that of the Antp complex with BS2. Another, difference is that the Antp homeodomain is more stable with respect to, thermal denaturation, with denaturation temperatures at pH 4.8 of 27, degrees C and 48 degrees C, respectively, for ftz and Antp.
+The three-dimensional structure of a recombinant 70-residue polypeptide containing the complete fushi tarazu (ftz) homeodomain from Drosophila melanogaster has been determined by nuclear magnetic resonance (NMR) spectroscopy in solution. On the basis of 915 upper distance constraints derived from nuclear Overhauser effects and 178 dihedral angle constraints, a group of 20 conformers representing the solution structure of the ftz homeodomain was computed with the program DIANA and energy-minimized with the program OPAL. The average of the pairwise root-mean-square deviations of the individual NMR conformers relative to the mean coordinates is 0.50 A for the backbone atoms N, C alpha and C' of residues 8 to 53. The molecular architecture includes three helices comprising the residues 10 to 21, 28 to 38, and 42 to 52, a loop of residues 22 to 27 between the helices I and II, and a turn of residues 39 to 41 linking the helices II and III. Comparisons with the structure of the mutant Antennapedia homeodomain with Cys39 replaced by Ser, Antp (C39S), shows that the two proteins contain the same molecular fold for residues 8 to 53, whereas the more flexible fourth helix comprising residues 53 to 59 in the Antp (C39S) homeodomain has no counterpart in the ftz homeodomain. Considering that important intermolecular interactions in the DNA complexes with the Antp, engrailed and Mat alpha 2 homeodomains involve the fourth helix, it was rather unexpected that the stability of the complex of ftz with the BS2 operator site was found to be comparable to or even somewhat higher than that of the Antp complex with BS2. Another difference is that the Antp homeodomain is more stable with respect to thermal denaturation, with denaturation temperatures at pH 4.8 of 27 degrees C and 48 degrees C, respectively, for ftz and Antp.
 ==About this Structure==
-FTZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FTZ OCA].
+FTZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FTZ OCA].
 ==Reference==
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 [[Category: Single protein]]
 [[Category: Furukubo-Tokunaga, K.]]
-[[Category: Gehring, W.J.]]
+[[Category: Gehring, W J.]]
 [[Category: Muller, M.]]
-[[Category: Qian, Y.Q.]]
+[[Category: Qian, Y Q.]]
 [[Category: Resendez-Perez, D.]]
 [[Category: Wuthrich, K.]]
 [[Category: dna-binding]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:16:54 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:42:42 2008''