1ovt
From Proteopedia
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|PDB= 1ovt |SIZE=350|CAPTION= <scene name='initialview01'>1ovt</scene>, resolution 2.4Å | |PDB= 1ovt |SIZE=350|CAPTION= <scene name='initialview01'>1ovt</scene>, resolution 2.4Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ovt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ovt OCA], [http://www.ebi.ac.uk/pdbsum/1ovt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ovt RCSB]</span> | ||
}} | }} | ||
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[[Category: Kurokawa, H.]] | [[Category: Kurokawa, H.]] | ||
[[Category: Mikami, B.]] | [[Category: Mikami, B.]] | ||
| - | [[Category: CO3]] | ||
| - | [[Category: FE]] | ||
[[Category: iron transport protein]] | [[Category: iron transport protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:51:04 2008'' |
Revision as of 19:51, 30 March 2008
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| , resolution 2.4Å | |||||||
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| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
REFINED CRYSTALLOGRAPHIC STRUCTURE OF HEN OVOTRANSFERRIN AT 2.4 ANGSTROMS RESOLUTION
Overview
The three-dimensional structure of diferric hen ovotransferrin has been determined by X-ray crystallography at 2.4 A resolution. The structure was solved by molecular replacement, using the coordinates of diferric human lactoferrin as a search model. Several rounds of simulated annealing and restrained least-squares refinement have resulted in a model structure with an R-factor of 0.171 for the data between 11.0 and 2.4 A resolution. The model comprises 5284 protein atoms (residues 5 to 686), 2 Fe3+, 2 CO3(2)- and 132 water molecules. The overall structure of ovotransferrin is similar to those of human lactoferrin and rabbit serum transferrin, being folded into two homologous lobes, each containing two dissimilar domains with one Fe3+ and one CO3(2)- bound at a specific site in each interdomain cleft. However, the relative orientation of the two lobes, which may be related to the class specificity of transferrins to receptors, is different from either human lactoferrin or rabbit serum transferrin. The angle of the relative orientation in ovotransferrin is increased by 6.8 degrees and 15.7 degrees as compared with to those in rabbit serum transferrin and human lactoferrin, respectively. Interdomain Lys209-Lys301 and Gln541-Lys638 interactions are found near the metal binding site of each lobe. The interlobe interactions and their role in the stabilization of iron binding are discussed.
About this Structure
1OVT is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
Reference
Crystal structure of diferric hen ovotransferrin at 2.4 A resolution., Kurokawa H, Mikami B, Hirose M, J Mol Biol. 1995 Nov 24;254(2):196-207. PMID:7490743
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