1dot

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[[Image:1dot.gif|left|200px]]
[[Image:1dot.gif|left|200px]]
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{{Structure
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|PDB= 1dot |SIZE=350|CAPTION= <scene name='initialview01'>1dot</scene>, resolution 2.35&Aring;
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The line below this paragraph, containing "STRUCTURE_1dot", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>
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{{STRUCTURE_1dot| PDB=1dot | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dot FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dot OCA], [http://www.ebi.ac.uk/pdbsum/1dot PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dot RCSB]</span>
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'''CRYSTALLOGRAPHIC STRUCTURE OF DUCK OVOTRANSFERRIN AT 2.3 ANGSTROMS RESOLUTION'''
'''CRYSTALLOGRAPHIC STRUCTURE OF DUCK OVOTRANSFERRIN AT 2.3 ANGSTROMS RESOLUTION'''
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[[Category: Muirhead, H.]]
[[Category: Muirhead, H.]]
[[Category: Rawas, A.]]
[[Category: Rawas, A.]]
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[[Category: iron transport protein]]
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[[Category: Iron transport protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:05:46 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:45:42 2008''
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Revision as of 11:05, 2 May 2008

Image:1dot.gif

Template:STRUCTURE 1dot

CRYSTALLOGRAPHIC STRUCTURE OF DUCK OVOTRANSFERRIN AT 2.3 ANGSTROMS RESOLUTION


Overview

The structure of diferric duck ovotransferrin (DOT) has been determined and refined at a resolution of 2.35 A. The DOT structure, which contains two iron binding sites, is similar to the known transferrin and lactoferrin structures. The two iron-binding sites, one in the N-terminal lobe and one in the C-terminal lobe of the molecule, are similar but not identical. The main differences between the three known structures lie in the relative orientations of the N- and C-lobes with respect to each other. In the DOT structure the large aromatic side chain of Phe322 in the N-lobe packs against the conserved residue Gly387 in the C-lobe. This interaction is at the centre of the interface between the two lobes and could play a crucial role in determining their relative orientation. Other differences between the structures occur in the surface loops and in the peptide connecting the two lobes. The final crystallographic model consists of 5309 protein atoms (686 residues), two Fe(3+) ions, two (bi)carbonate ions and three carbohydrate moities. 318 water molecules have been added to the model. The final R factor is 0.22 for 25 400 observed reflections between 10 and 2.35 A resolution.

About this Structure

1DOT is a Single protein structure of sequence from Anas platyrhynchos. Full crystallographic information is available from OCA.

Reference

Structure of diferric duck ovotransferrin at 2.35 A resolution., Rawas A, Muirhead H, Williams J, Acta Crystallogr D Biol Crystallogr. 1996 Jul 1;52(Pt 4):631-40. PMID:15299626 Page seeded by OCA on Fri May 2 14:05:46 2008

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