5ina | pdb_00005ina

Chaperone Spy bound to Im7 6-45 ensemble

spinqualitylabelsall models 5ina, resolution 1.79Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ina is a 3 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: IMD, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [SPY_ECOLI] An ATP-independent periplasmic chaperone, decreases protein aggregation and helps protein refolding. Binds substrate over a large region of its convex inner surface (PubMed:21317898, PubMed:24497545). Substrate protein folds while it is bound to chaperone (PubMed:26619265). Increasing Spy flexibility increases its substrate affinity and overall chaperone activity (shown for 3 different substrates) (PubMed:24497545). Protects proteins in vitro against tannin inactivation; tannins have antimicrobial activity (PubMed:21317898). Overexpression enhances the stability of otherwise unstable periplasmic proteins (PubMed:21317898). [IMM7_ECOLX] This protein is able to protect a cell, which harbors the plasmid ColE7 encoding colicin E7, against colicin E7, it binds specifically to the DNase-type colicin and inhibits its bactericidal activity. Dimeric ImmE7 may possess a RNase activity that cleaves its own mRNA at a specific site and thus autoregulates translational expression of the downstream ceiE7 gene as well as degradation of the upstream ceaE7 mRNA.

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