1tl4
From Proteopedia
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|PDB= 1tl4 |SIZE=350|CAPTION= <scene name='initialview01'>1tl4</scene> | |PDB= 1tl4 |SIZE=350|CAPTION= <scene name='initialview01'>1tl4</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CU1:COPPER (I) ION'>CU1</scene> | + | |LIGAND= <scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= ATOX1, HAH1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= ATOX1, HAH1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1tl5|1TL5]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tl4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tl4 OCA], [http://www.ebi.ac.uk/pdbsum/1tl4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tl4 RCSB]</span> | ||
}} | }} | ||
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[[Category: Rosato, A.]] | [[Category: Rosato, A.]] | ||
[[Category: SPINE, Structural Proteomics in Europe.]] | [[Category: SPINE, Structural Proteomics in Europe.]] | ||
| - | [[Category: CU1]] | ||
[[Category: copper chaperone]] | [[Category: copper chaperone]] | ||
[[Category: copper protein]] | [[Category: copper protein]] | ||
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[[Category: wilson]] | [[Category: wilson]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:57:35 2008'' |
Revision as of 20:57, 30 March 2008
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| Ligands: | |||||||
| Gene: | ATOX1, HAH1 (Homo sapiens) | ||||||
| Related: | 1TL5
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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