Journal:JBIC:14
From Proteopedia
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<StructureSection load='2kr7' size='500' side='right' scene='Journal:JBIC:14/Cv/1' caption=''> | <StructureSection load='2kr7' size='500' side='right' scene='Journal:JBIC:14/Cv/1' caption=''> | ||
- | === Multifaceted SlyD from Helicobacter pylori: implication in [NiFe] hydrogenase maturation === | + | === Multifaceted SlyD from ''Helicobacter pylori'': implication in [NiFe] hydrogenase maturation === |
<big>Tianfan Cheng, Hongyan Li, Wei Xia1 and Hongzhe Sun</big><ref >DOI 10.1007/s00775-011-0855-y</ref> | <big>Tianfan Cheng, Hongyan Li, Wei Xia1 and Hongzhe Sun</big><ref >DOI 10.1007/s00775-011-0855-y</ref> | ||
<hr/> | <hr/> | ||
<b>Molecular Tour</b><br> | <b>Molecular Tour</b><br> | ||
- | 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., | + | 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., Ni<sup>2+</sup>, Zn<sup>2+</sup>), 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'' (HpSlyDΔC). HpSlyDΔC 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 β-sheet with an α-helix on one side, whereas the IF domain folds into a four-stranded antiparallel β-sheet accompanied by a short α-helix. Intact ''H. pylori'' SlyD binds both Ni<sup>2+</sup> and Zn<sup>2+</sup>, with dissociation constants of 2.74 and 3.79 μM respectively. Intriguingly, binding of Ni<sup>2+</sup> instead of Zn<sup>2+</sup> 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. |
</StructureSection> | </StructureSection> |
Revision as of 09:18, 17 November 2011
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- ↑ Cheng T, Li H, Xia W, Sun H. Multifaceted SlyD from Helicobacter pylori: implication in [NiFe] hydrogenase maturation. J Biol Inorg Chem. 2011 Nov 2. PMID:22045417 doi:10.1007/s00775-011-0855-y
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