1dot
From Proteopedia
(New page: 200px<br /><applet load="1dot" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dot, resolution 2.35Å" /> '''CRYSTALLOGRAPHIC STR...) |
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| - | [[Image:1dot.gif|left|200px]]<br /><applet load="1dot" size=" | + | [[Image:1dot.gif|left|200px]]<br /><applet load="1dot" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1dot, resolution 2.35Å" /> | caption="1dot, resolution 2.35Å" /> | ||
'''CRYSTALLOGRAPHIC STRUCTURE OF DUCK OVOTRANSFERRIN AT 2.3 ANGSTROMS RESOLUTION'''<br /> | '''CRYSTALLOGRAPHIC STRUCTURE OF DUCK OVOTRANSFERRIN AT 2.3 ANGSTROMS RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of diferric duck ovotransferrin (DOT) has been determined | + | 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== | ==About this Structure== | ||
| - | 1DOT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Anas_platyrhynchos Anas platyrhynchos] with NAG, FUC, FE and CO3 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1DOT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Anas_platyrhynchos Anas platyrhynchos] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=FUC:'>FUC</scene>, <scene name='pdbligand=FE:'>FE</scene> and <scene name='pdbligand=CO3:'>CO3</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DOT OCA]. |
==Reference== | ==Reference== | ||
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[[Category: iron transport protein]] | [[Category: iron transport protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:18:51 2008'' |
Revision as of 10:18, 21 February 2008
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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 with , , and as ligands. 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 Thu Feb 21 12:18:51 2008
Categories: Anas platyrhynchos | Single protein | Muirhead, H. | Rawas, A. | CO3 | FE | FUC | NAG | Iron transport protein
