2VB3

Crystal structure of Ag(I)CusF

Summary for 2VB3

Entry DOI	10.2210/pdb2vb3/pdb
Related	1ZEQ 2VB2
Descriptor	CATION EFFLUX SYSTEM PROTEIN CUSF, SILVER ION (3 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	9974.09
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 Cited by 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 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.33 Å)

Structure validation