2VB2

Crystal structure of Cu(I)CusF

Summary for 2VB2

• Entry DOI: 10.2210/pdb2vb2/pdb
• Related: 1ZEQ 2VB3
• Descriptor: CATION EFFLUX SYSTEM PROTEIN CUSF, SULFATE ION, COPPER (II) ION, ... (4 entities in total)
• Functional Keywords: cation pi, metal-binding, metal transport, copper tolerance, copper transport
• Biological source: ESCHERICHIA COLI
• Cellular location: Periplasm: P77214
• Total number of polymer chains: 1
• Total formula weight: 10025.83

Authors

Xue, Y.,Davis, A.V.,Balakrishnan, G.,Stasser, J.P.,Staehlin, B.M.,Focia, P.,Spiro, T.G.,Penner-Hahn, J.E.,O'Halloran, T.V. (deposition date: 2007-09-06, release date: 2007-12-18, Last modification date: 2023-12-13)

Primary citation

Xue, Y.,Davis, A.V.,Balakrishnan, G.,Stasser, J.P.,Staehlin, B.M.,Focia, P.,Spiro, T.G.,Penner-Hahn, J.E.,O'Halloran, T.V.
Cu(I) Recognition Via Cation-Pi and Methionine Interactions in Cusf.
Nat.Chem.Biol., 4:107-, 2008

PubMed Abstract: Methionine-rich motifs have an important role in copper trafficking factors, including the CusF protein. Here we show that CusF uses a new metal recognition site wherein Cu(I) is tetragonally displaced from a Met2His ligand plane toward a conserved tryptophan. Spectroscopic studies demonstrate that both thioether ligation and strong cation-pi interactions with tryptophan stabilize metal binding. This novel active site chemistry affords mechanisms for control of adventitious metal redox and substitution chemistry.

PubMed: 18157124
DOI: 10.1038/NCHEMBIO.2007.57

Experimental method

X-RAY DIFFRACTION (1.7 Å)