期刊
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY
卷 17, 期 3, 页码 331-343出版社
SPRINGER
DOI: 10.1007/s00775-011-0855-y
关键词
Chaperone; Hydrogenase; NMR; Peptidylprolyl isomerase; SlyD
资金
- Research Grants Council of Hong Kong [HKU107C, HKU704207P, HKU703808P, HKU704909P, N_HKU75209]
- Croucher Foundation
- University of Hong Kong
- University Grants Committee of the Hong Kong Special Administrative Region, China [SEG_HKU02]
SlyD belongs to the FK506-binding protein (FKBP) family with both peptidylprolyl isomerase (PPIase) and chaperone activities, and is considered to be a ubiquitous cytosolic protein-folding facilitator in bacteria. It possesses a histidine- and cysteine-rich C-terminus binding to selected divalent metal ions (e.g., Ni2+, Zn2+), which is important for its involvement in the maturation processes of metalloenzymes. We have determined the solution structure of C-terminus-truncated SlyD from Helicobacter pylori (HpSlyD Delta C). HpSlyD Delta C folds into two well-separated, orientation-independent domains: the PPIase-active FKBP domain and the chaperone-active insert-in-flap (IF) domain. The FKBP domain consists of a four-stranded antiparallel beta-sheet with an alpha-helix on one side, whereas the IF domain folds into a four-stranded antiparallel beta-sheet accompanied by a short alpha-helix. Intact H. pylori SlyD binds both Ni2+ and Zn2+, with dissociation constants of 2.74 and 3.79 mu M respectively. Intriguingly, binding of Ni2+ instead of Zn2+ induces protein conformational changes around the active sites of the FKBP domain, implicating a regulatory role of nickel. The twin-arginine translocation (Tat) signal peptide from the small subunit of [NiFe] hydrogenase (HydA) binds the protein at the IF domain. Nickel binding and the recognition of the Tat signal peptide by the protein suggest that SlyD participates in [NiFe] hydrogenase maturation processes.
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