2.A.5.1.22 Zinc (ZrfC) transporter of 522 aas and 9 TMSs in a 1 (N-terminal) + 3 (central; residues 200 - 300) + 5 TMSs (C-terminal). Aspergillus fumigatus, one of the most widespread opportunistic human fungal pathogens, adapts to zinc limitation by secreting a 310 amino acid Aspf2 zincophore, able to specifically bind Zn2+ and deliver it to ZrfC. Garstka et al. 2022 focused on the thermodynamics of Zn2+ complexes with unstructured regions of Aspf2; basing on a variety of spectrometric and potentiometric data, they show that the C-terminal part has the highest Zn(II)-binding affinity among the potential binding sites, and Ni2+ does not compete with Zn2+ binding to this region. The 14 amino acid Aspf2 C-terminus coordinates Zn2+ via two Cys thiolates and two His imidazoles (Garstka et al. 2022). The Aspf2 zincophore protein is a member of the Asp F2 family (TC# 8.A.190).
|
Accession Number: | D3W9Z7 |
Protein Name: | Aspf2 |
Length: | 310 |
Molecular Weight: | 32862.00 |
Species: | Neosartorya fumigata (Aspergillus fumigatus) [746128] |
Number of TMSs: | 1 |
Substrate |
zinc(2+) |
---|
1: MAALLRLAVL LPLAAPLVAT LPTSPVPIAA RATPHEPVFF SWDAGAVTSF PIHSSCNATQ
61: RRQIEAGLNE AVELARHAKA HILRWGNESE IYRKYFGNRP TMEAVGAYDV IVNGDKANVL
121: FRCDNPDGNC ALEGWGGHWR GANATSETVI CDRSYTTRRW LVSMCSQGYT VAGSETNTFW
181: ASDLMHRLYH VPAVGQGWVD HFADGYDEVI ALAKSNGTES THDSEALQYF ALEAYAFDIA
241: APGVGCAGES HGPDQGHDTG SASAPASTST SSSSSASGSG ATTTPTDSPS ATIDVPPNCH
301: THEGGQLHCT