1tl4
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(New page: 200px<br /> <applet load="1tl4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tl4" /> '''Solution structure of Cu(I) HAH1'''<br /> ...)
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Revision as of 17:19, 12 November 2007
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Solution structure of Cu(I) HAH1
Overview
The human metallochaperone HAH1 has been produced in Escherichia coli with, four additional amino acids at the C-terminus and characterized in, solution by NMR spectroscopy, both with and without copper(I). The, solution structure of the apo-HAH1 monomer has a, root-mean-square-deviation (RMSD) of 0.50 A for the coordinates of the, backbone atoms and 0.96 A for all heavy atoms. These values compare, respectively, with 0.45 and 0.95 A for copper(I)-HAH1. There are only, minor structural rearrangements upon copper(I) binding. In particular, the, variation of interatomic interactions around the metal-binding region is, limited to a movement of Lys60 toward the metal site. The protein, structures are similar to those obtained by X-ray crystallography in a, variety of derivatives, with backbone RMSD values below 1 A. In the, holoprotein, copper(I) is confirmed to be two coordinated. If these data, are compared with those of orthologue proteins, we learn that HAH1 has a, lower tendency to change coordination number from two to three. Such a, switch in coordination is a key step in copper transfer.
About this Structure
1TL4 is a Single protein structure of sequence from Homo sapiens with CU1 as ligand. Full crystallographic information is available from OCA.
Reference
Solution structure of the apo and copper(I)-loaded human metallochaperone HAH1., Anastassopoulou I, Banci L, Bertini I, Cantini F, Katsari E, Rosato A, Biochemistry. 2004 Oct 19;43(41):13046-53. PMID:15476398
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