| Structural highlights
Function
HDEA_ECOLI Required for optimal acid stress protection. Exhibits a chaperone-like activity only at pH below 3 by suppressing non-specifically the aggregation of denaturated periplasmic proteins. Important for survival of enteric bacteria in the acidic environment of the host stomach. Also promotes the solubilization at neutral pH of proteins that had aggregated in their presence at acidic pHs. May cooperate with other periplasmic chaperones such as DegP and SurA.[1] [2] [3] [4]
References
- ↑ Hong W, Jiao W, Hu J, Zhang J, Liu C, Fu X, Shen D, Xia B, Chang Z. Periplasmic protein HdeA exhibits chaperone-like activity exclusively within stomach pH range by transforming into disordered conformation. J Biol Chem. 2005 Jul 22;280(29):27029-34. Epub 2005 May 23. PMID:15911614 doi:http://dx.doi.org/M503934200
- ↑ Kern R, Malki A, Abdallah J, Tagourti J, Richarme G. Escherichia coli HdeB is an acid stress chaperone. J Bacteriol. 2007 Jan;189(2):603-10. Epub 2006 Nov 3. PMID:17085547 doi:http://dx.doi.org/10.1128/JB.01522-06
- ↑ Malki A, Le HT, Milles S, Kern R, Caldas T, Abdallah J, Richarme G. Solubilization of protein aggregates by the acid stress chaperones HdeA and HdeB. J Biol Chem. 2008 May 16;283(20):13679-87. Epub 2008 Mar 20. PMID:18359765 doi:http://dx.doi.org/M800869200
- ↑ Zhang M, Lin S, Song X, Liu J, Fu Y, Ge X, Fu X, Chang Z, Chen PR. A genetically incorporated crosslinker reveals chaperone cooperation in acid resistance. Nat Chem Biol. 2011 Sep 4;7(10):671-7. doi: 10.1038/nchembio.644. PMID:21892184 doi:http://dx.doi.org/10.1038/nchembio.644
|
