1bka: Difference between revisions
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==About this Structure== | ==About this Structure== | ||
1BKA is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with FE and OXL as [[http://en.wikipedia.org/wiki/ligands ligands]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BKA OCA]]. | 1BKA is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with FE and OXL as [[http://en.wikipedia.org/wiki/ligands ligands]]. Structure known Active Sites: AN1, AN2, FE1 and FE2. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BKA OCA]]. | ||
==Reference== | ==Reference== | ||
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[[Category: iron binding protein]] | [[Category: iron binding protein]] | ||
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Revision as of 15:02, 30 October 2007
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OXALATE-SUBSTITUTED DIFERRIC LACTOFERRIN
OverviewOverview
Proteins of the transferrin family bind, with high affinity, two Fe3+ ions, and two CO3(2)- ions but can also bind other metal ions and other anions., In order to find out how the protein structure and its two binding sites, adapt to the binding of larger anions, we have determined the crystal, structure of oxalate-substituted diferric lactoferrin at 2.4 A resolution., The final model has a crystallographic R-factor of 0.196 for all data in, the range 8.0-2.4 A. Substitution of oxalate for carbonate does not, produce any significant change in the polypeptide folding or domain, closure. Both binding sites are perturbed, however, and the effects are, different in each. In the C-lobe site the oxalate ion is bound to iron in, symmetric 1,2-bidentate fashion whereas in the N-lobe the anion, ... [(full description)]
About this StructureAbout this Structure
1BKA is a [Single protein] structure of sequence from [Homo sapiens] with FE and OXL as [ligands]. Structure known Active Sites: AN1, AN2, FE1 and FE2. Full crystallographic information is available from [OCA].
ReferenceReference
Anion binding by transferrins: importance of second-shell effects revealed by the crystal structure of oxalate-substituted diferric lactoferrin., Baker HM, Anderson BF, Brodie AM, Shongwe MS, Smith CA, Baker EN, Biochemistry. 1996 Jul 16;35(28):9007-13. PMID:8703903
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