1tl4

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[[Image:1tl4.jpg|left|200px]]
[[Image:1tl4.jpg|left|200px]]
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{{Structure
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|PDB= 1tl4 |SIZE=350|CAPTION= <scene name='initialview01'>1tl4</scene>
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The line below this paragraph, containing "STRUCTURE_1tl4", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|GENE= ATOX1, HAH1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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{{STRUCTURE_1tl4| PDB=1tl4 | SCENE= }}
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|RELATEDENTRY=[[1tl5|1TL5]]
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|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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'''Solution structure of Cu(I) HAH1'''
'''Solution structure of Cu(I) HAH1'''
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[[Category: Rosato, A.]]
[[Category: Rosato, A.]]
[[Category: SPINE, Structural Proteomics in Europe.]]
[[Category: SPINE, Structural Proteomics in Europe.]]
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[[Category: copper chaperone]]
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[[Category: Copper chaperone]]
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[[Category: copper protein]]
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[[Category: Copper protein]]
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[[Category: menke]]
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[[Category: Menke]]
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[[Category: spine]]
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[[Category: Spine]]
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[[Category: structural genomic]]
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[[Category: Structural genomic]]
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[[Category: structural proteomics in europe]]
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[[Category: Structural proteomics in europe]]
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[[Category: wilson]]
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[[Category: Wilson]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Apr 13 08:11:54 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:57:35 2008''
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Revision as of 05:11, 13 April 2008

Template:STRUCTURE 1tl4

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 Page seeded by OCA on Sun Apr 13 08:11:54 2008

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