1vfd: Difference between revisions
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==Overview== | ==Overview== | ||
A conserved arginine residue helps to form the synergistic anion binding, site in transferrins. To probe the importance of this residue for anion, binding and iron binding, Arg 121 has been mutated to Ser and Glu in, N-terminal half-molecule of human lactoferrin. The two mutants, R121S and, R121E, have been expressed, purified, and crystallized. Their, three-dimensional structures have been determined by X-ray diffraction at, 2.3 and 2.5 A resolution, respectively. The structures were determined by, molecular replacement and were refined by restrained least squares methods, to final R values of 0.185 and 0.204. Both mutants still bind iron but, with decreased stability. The crystal structures show that destabilization, of iron binding probably results from disruption of the anion binding, ... | A conserved arginine residue helps to form the synergistic anion binding, site in transferrins. To probe the importance of this residue for anion, binding and iron binding, Arg 121 has been mutated to Ser and Glu in, N-terminal half-molecule of human lactoferrin. The two mutants, R121S and, R121E, have been expressed, purified, and crystallized. Their, three-dimensional structures have been determined by X-ray diffraction at, 2.3 and 2.5 A resolution, respectively. The structures were determined by, molecular replacement and were refined by restrained least squares methods, to final R values of 0.185 and 0.204. Both mutants still bind iron but, with decreased stability. The crystal structures show that destabilization, of iron binding probably results from disruption of the anion binding, site; mutation of Arg 121 removes one wall of the anion binding pocket and, causes the synergistic carbonate ion to be displaced 0.5 A from its, position in the wild-type protein. In the process it becomes partially, detached from the helix N-terminus that forms the rest of the anion, binding site. | ||
==About this Structure== | ==About this Structure== | ||
1VFD is a | 1VFD 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 CO3 as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: BST. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1VFD OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: transferrin]] | [[Category: transferrin]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 12:54:05 2007'' | ||