Structural highlights
Function[MALE_ECOLI] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides. Publication Abstract from PubMedThe sensor histidine kinases of two-component signal-transduction systems (TCSs) are essential for bacteria to adapt to variable environmental conditions. The two-component regulatory system BaeS/R increases multidrug and metal resistance in Salmonella and Escherichia coli. In this study, we report the X-ray structure of the periplasmic sensor domain of BaeS from Serratia marcescens FS14. The BaeS sensor domain (34-160) adopts a mixed alpha/beta-fold containing a central four-stranded antiparallel beta-sheet flanked by a long N-terminal alpha-helix and additional loops and a short C-terminal alpha-helix on each side. Structural comparisons revealed that it belongs to the PDC family with a remarkable difference in the orientation of the helix alpha2. In the BaeS sensor domain, this helix is situated perpendicular to the long helix alpha1 and holds helix alpha1 in the middle with the beta sheet, whereas in other PDC domains, helix alpha2 is parallel to helix alpha1. Because the helices alpha1 and alpha2 is involved in the dimeric interface, this difference implies that BaeS uses a different dimeric interface compared with other PDC domains. Proteins 2017; 85:1784-1790. (c) 2017 Wiley Periodicals, Inc. Crystal structure of the sensor domain of BaeS from Serratia marcescens FS14.,Zhang Y, Qiu S, Jia S, Xu D, Ran T, Wang W Proteins. 2017 Sep;85(9):1784-1790. doi: 10.1002/prot.25326. Epub 2017 Jun 7. PMID:28544098[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||||||
This page was last modified 12:24, 16 January 2019.