1TL5

Solution structure of apoHAH1

Summary for 1TL5

• Entry DOI: 10.2210/pdb1tl5/pdb
• Descriptor: Copper transport protein ATOX1 (1 entity in total)
• Functional Keywords: copper protein, copper chaperone, menkes, wilson, structural proteomics in europe, spine, structural genomics, metal transport
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 7412.65

Authors

Anastassopoulou, I.,Banci, L.,Bertini, I.,Cantini, F.,Katsari, E.,Rosato, A.,Structural Proteomics in Europe (SPINE) (deposition date: 2004-06-09, release date: 2004-10-26, Last modification date: 2024-05-22)

Primary citation

Anastassopoulou, I.,Banci, L.,Bertini, I.,Cantini, F.,Katsari, E.,Rosato, A.
Solution Structure of the Apo and Copper(I)-Loaded Human Metallochaperone HAH1.
Biochemistry, 43:13046-13053, 2004

PubMed Abstract: 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.

PubMed: 15476398
DOI: 10.1021/bi0487591

Experimental method

SOLUTION NMR