2myj

Solution structure of a bacterial chaperone

spinqualitylabelsall models 2myj, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2myj is a 2 chain structure with sequence from Ecoli. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: hdeB, yhhD, yhiC, b3509, JW5669 (ECOLI) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [HDEB_ECOLI] Required for optimal acid stress protection, which is important for survival of enteric bacteria in the acidic environment of the host stomach. Exhibits a chaperone-like activity at acidic pH by preventing the aggregation of many different periplasmic proteins. Publication Abstract from PubMed Enteric bacteria encounter extreme acidity when passing through hosts' stomach. Since the bacterial periplasmic space quickly equilibrates with outer environment, an efficient acid resistance mechanism is essential in preventing irreversible protein denaturation/aggregation and maintaining bacteria viability. HdeB, along with its homolog HdeA, was identified as a periplasmic acid-resistant chaperone. Both proteins exist as homodimers and share similar monomeric structures under neutral pH, while showing different dimeric packing interfaces. Previous investigations show that HdeA functions through an acid-induced dimer-to-monomer transition and partial unfolding at low pH (pH 2-3), resulting in exposure of hydrophobic surfaces that bind substrate proteins. In contrast, HdeB appears to have a much higher optimal activation pH (pH 4-5), under which condition the protein maintains a well-folded dimer and the mechanism for its chaperone activity remains elusive. Herein, we present an NMR study of HdeB to investigate its dynamic properties. Our results reveal that HdeB undergoes significant micro- to milli-second timescale conformational exchanges at neutral to near-neutral pH, under the later condition it exhibits optimal activity. The current study indicates that HdeB activation is coupled to its intrinsic dynamics instead of structural changes, and therefore its functional mechanism is apparently different from HdeA. HdeB chaperone activity is coupled to its intrinsic dynamic properties.,Ding J, Yang C, Niu X, Hu Y, Jin C Sci Rep. 2015 Nov 23;5:16856. doi: 10.1038/srep16856. PMID:26593705 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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