1utg
From Proteopedia
(New page: 200px<br /><applet load="1utg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1utg, resolution 1.34Å" /> '''REFINEMENT OF THE C2...) |
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| - | [[Image:1utg.gif|left|200px]]<br /><applet load="1utg" size=" | + | [[Image:1utg.gif|left|200px]]<br /><applet load="1utg" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1utg, resolution 1.34Å" /> | caption="1utg, resolution 1.34Å" /> | ||
'''REFINEMENT OF THE C2221 CRYSTAL FORM OF OXIDIZED UTEROGLOBIN AT 1.34 ANGSTROMS RESOLUTION'''<br /> | '''REFINEMENT OF THE C2221 CRYSTAL FORM OF OXIDIZED UTEROGLOBIN AT 1.34 ANGSTROMS RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of uteroglobin, a progesterone binding protein from rabbit | + | The structure of uteroglobin, a progesterone binding protein from rabbit uterine fluid, was determined and refined at 1.34 A resolution to a conventional R-factor of 0.229. The accuracy of the co-ordinates is estimated to be 0.15 A. The isotropic temperature factor of individual atoms was refined and its average value is 11.9 A2 for the 548 non-hydrogen atoms of the protein monomer. A total of 83 water molecules was located in difference electron density maps and refined, first using a constant occupancy factor of 1 and then variable occupancy, the final (Q) being 0.63. The mean temperature factor of the water oxygen atoms is 26.4 A2. Uteroglobin is a dimer and its secondary structure consists of four alpha-helices per monomer that align in an anti-parallel fashion. There is one beta-turn between helix 2 and helix 3 (Lys26 to Glu29); 76% of the residues are part of the alpha-helices. In the core of the dimeric protein molecule, between the two monomers that are held together by two disulfide bridges, we have observed a closed cavity. Its length is 15.6 A and its width is 9 A; 14 water molecules could be positioned inside. In the "bottom" part of the protein, near the C terminus, we have observed a smaller cavity, occupied by two water molecules. The calculation of the molecular surface revealed four surface pockets whose possible functional implications are discussed below. |
==About this Structure== | ==About this Structure== | ||
| - | 1UTG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http:// | + | 1UTG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UTG OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Buehner, M.]] | [[Category: Buehner, M.]] | ||
[[Category: Morize, I.]] | [[Category: Morize, I.]] | ||
| - | [[Category: Mornon, J | + | [[Category: Mornon, J P.]] |
[[Category: Surcouf, E.]] | [[Category: Surcouf, E.]] | ||
| - | [[Category: Vaney, M | + | [[Category: Vaney, M C.]] |
[[Category: steroid binding]] | [[Category: steroid binding]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:28:11 2008'' |
Revision as of 13:28, 21 February 2008
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REFINEMENT OF THE C2221 CRYSTAL FORM OF OXIDIZED UTEROGLOBIN AT 1.34 ANGSTROMS RESOLUTION
Overview
The structure of uteroglobin, a progesterone binding protein from rabbit uterine fluid, was determined and refined at 1.34 A resolution to a conventional R-factor of 0.229. The accuracy of the co-ordinates is estimated to be 0.15 A. The isotropic temperature factor of individual atoms was refined and its average value is 11.9 A2 for the 548 non-hydrogen atoms of the protein monomer. A total of 83 water molecules was located in difference electron density maps and refined, first using a constant occupancy factor of 1 and then variable occupancy, the final (Q) being 0.63. The mean temperature factor of the water oxygen atoms is 26.4 A2. Uteroglobin is a dimer and its secondary structure consists of four alpha-helices per monomer that align in an anti-parallel fashion. There is one beta-turn between helix 2 and helix 3 (Lys26 to Glu29); 76% of the residues are part of the alpha-helices. In the core of the dimeric protein molecule, between the two monomers that are held together by two disulfide bridges, we have observed a closed cavity. Its length is 15.6 A and its width is 9 A; 14 water molecules could be positioned inside. In the "bottom" part of the protein, near the C terminus, we have observed a smaller cavity, occupied by two water molecules. The calculation of the molecular surface revealed four surface pockets whose possible functional implications are discussed below.
About this Structure
1UTG is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.
Reference
Refinement of the C222(1) crystal form of oxidized uteroglobin at 1.34 A resolution., Morize I, Surcouf E, Vaney MC, Epelboin Y, Buehner M, Fridlansky F, Milgrom E, Mornon JP, J Mol Biol. 1987 Apr 20;194(4):725-39. PMID:3656405
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