1tl5
From Proteopedia
(New page: 200px<br /> <applet load="1tl5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tl5" /> '''Solution structure of apoHAH1'''<br /> ==O...) |
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'''Solution structure of apoHAH1'''<br /> | '''Solution structure of apoHAH1'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1TL5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1TL5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TL5 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: wilson]] | [[Category: wilson]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:57:39 2008'' |
Revision as of 14:57, 15 February 2008
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Solution structure of apoHAH1
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
1TL5 is a Single protein structure of sequence from Homo sapiens. 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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