1utg: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 1: Line 1:
[[Image:1utg.gif|left|200px]]
[[Image:1utg.gif|left|200px]]


{{Structure
<!--
|PDB= 1utg |SIZE=350|CAPTION= <scene name='initialview01'>1utg</scene>, resolution 1.34&Aring;
The line below this paragraph, containing "STRUCTURE_1utg", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)
|LIGAND=  
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY=  
or leave the SCENE parameter empty for the default display.
|GENE=
-->
|DOMAIN=
{{STRUCTURE_1utg| PDB=1utg  | SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1utg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1utg OCA], [http://www.ebi.ac.uk/pdbsum/1utg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1utg RCSB]</span>
}}


'''REFINEMENT OF THE C2221 CRYSTAL FORM OF OXIDIZED UTEROGLOBIN AT 1.34 ANGSTROMS RESOLUTION'''
'''REFINEMENT OF THE C2221 CRYSTAL FORM OF OXIDIZED UTEROGLOBIN AT 1.34 ANGSTROMS RESOLUTION'''
Line 30: Line 27:
[[Category: Surcouf, E.]]
[[Category: Surcouf, E.]]
[[Category: Vaney, M C.]]
[[Category: Vaney, M C.]]
[[Category: steroid binding]]
[[Category: Steroid binding]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 11:39:56 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:14:58 2008''

Revision as of 11:39, 3 May 2008

File:1utg.gif

Template:STRUCTURE 1utg

REFINEMENT OF THE C2221 CRYSTAL FORM OF OXIDIZED UTEROGLOBIN AT 1.34 ANGSTROMS RESOLUTION


OverviewOverview

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 StructureAbout this Structure

1UTG is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.

ReferenceReference

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 Page seeded by OCA on Sat May 3 11:39:56 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA