1CC8

CRYSTAL STRUCTURE OF THE ATX1 METALLOCHAPERONE PROTEIN

Summary for 1CC8

• Entry DOI: 10.2210/pdb1cc8/pdb
• Descriptor: PROTEIN (METALLOCHAPERONE ATX1), MERCURY (II) ION, BENZAMIDINE, ... (4 entities in total)
• Functional Keywords: copper transport, mercury coordination, metal transport
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Cytoplasm: P38636
• Total number of polymer chains: 1
• Total formula weight: 8673.54

Authors

Rosenzweig, A.C.,Huffman, D.L.,Pufahl, M.Y.R.A.,Hou, T.V.O.,Wernimont, A.K. (deposition date: 1999-03-04, release date: 1999-12-12, Last modification date: 2023-12-27)

Primary citation

Rosenzweig, A.C.,Huffman, D.L.,Hou, M.Y.,Wernimont, A.K.,Pufahl, R.A.,O'Halloran, T.V.
Crystal structure of the Atx1 metallochaperone protein at 1.02 A resolution.
Structure Fold.Des., 7:605-617, 1999

PubMed Abstract: Metallochaperone proteins function in the trafficking and delivery of essential, yet potentially toxic, metal ions to distinct locations and particular proteins in eukaryotic cells. The Atx1 protein shuttles copper to the transport ATPase Ccc2 in yeast cells. Molecular mechanisms for copper delivery by Atx1 and similar human chaperones have been proposed, but detailed structural characterization is necessary to elucidate how Atx1 binds metal ions and how it might interact with Ccc2 to facilitate metal ion transfer.

PubMed: 10404590
DOI: 10.1016/S0969-2126(99)80082-3

Experimental method

X-RAY DIFFRACTION (1.02 Å)