1aiv
From Proteopedia
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| - | [[Image:1aiv.gif|left|200px]] | + | [[Image:1aiv.gif|left|200px]] |
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| - | '''APO OVOTRANSFERRIN''' | + | {{Structure |
| + | |PDB= 1aiv |SIZE=350|CAPTION= <scene name='initialview01'>1aiv</scene>, resolution 3.Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''APO OVOTRANSFERRIN''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1AIV is a [ | + | 1AIV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AIV OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of hen apo-ovotransferrin. Both lobes adopt an open conformation upon loss of iron., Kurokawa H, Dewan JC, Mikami B, Sacchettini JC, Hirose M, J Biol Chem. 1999 Oct 1;274(40):28445-52. PMID:[http:// | + | Crystal structure of hen apo-ovotransferrin. Both lobes adopt an open conformation upon loss of iron., Kurokawa H, Dewan JC, Mikami B, Sacchettini JC, Hirose M, J Biol Chem. 1999 Oct 1;274(40):28445-52. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10497206 10497206] |
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: iron transport protein]] | [[Category: iron transport protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:58:09 2008'' |
Revision as of 07:58, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
APO OVOTRANSFERRIN
Overview
The three-dimensional crystal structure of hen apo-ovotransferrin has been solved by molecular replacement and refined by simulated annealing and restrained least squares to a 3.0-A resolution. The final model, which comprises 5312 protein atoms (residues 1 to 686) and 28 carbohydrate atoms (from two monosaccharides attached to Asn(473)), gives an R-factor of 0.231 for the 11,989 observed reflections between 20.0- and 3.0-A resolution. In the structure, both empty iron binding clefts are in the open conformation, lending weight to the theory that Fe(3+) binding or release in transferrin proceeds via a mechanism that involves domain opening and closure. Upon opening, the domains rotate essentially as rigid bodies. The two domains of the N-lobe rotate away from one another by 53 degrees, whereas the C-lobe domains rotate away each another by 35 degrees. These rotations take place about an axis that passes through the two beta-strands, linking the domains. The domains of each lobe make different contacts with one another in the open and closed forms. These contacts form two interdomain interfaces on either side of the rotation axis, and domain opening or closing produces a see-saw motion between these two alternative close-packed interfaces. The interdomain disulfide bridge (Cys(478)-Cys(671)), found only in the C-lobe, may restrict domain opening but does not completely prevent it.
About this Structure
1AIV is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
Reference
Crystal structure of hen apo-ovotransferrin. Both lobes adopt an open conformation upon loss of iron., Kurokawa H, Dewan JC, Mikami B, Sacchettini JC, Hirose M, J Biol Chem. 1999 Oct 1;274(40):28445-52. PMID:10497206
Page seeded by OCA on Thu Mar 20 09:58:09 2008
