1tl5: Difference between revisions
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'''Solution structure of apoHAH1''' | {{Structure | ||
|PDB= 1tl5 |SIZE=350|CAPTION= <scene name='initialview01'>1tl5</scene> | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= ATOX1, HAH1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |||
}} | |||
'''Solution structure of apoHAH1''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1TL5 is a [ | 1TL5 is a [[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== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15476398 15476398] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: copper chaperone]] | [[Category: copper chaperone]] | ||
[[Category: copper protein]] | [[Category: copper protein]] | ||
[[Category: | [[Category: menke]] | ||
[[Category: spine]] | [[Category: spine]] | ||
[[Category: structural | [[Category: structural genomic]] | ||
[[Category: structural proteomics in europe]] | [[Category: structural proteomics in europe]] | ||
[[Category: wilson]] | [[Category: wilson]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:19:51 2008'' | ||
Revision as of 12:19, 20 March 2008
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| 1tl5 | |||||||||||||
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| Gene: | ATOX1, HAH1 (Homo sapiens) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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
Page seeded by OCA on Thu Mar 20 14:19:51 2008
