Show simple item record

dc.contributor.authorLin, Yuchun
dc.contributor.authorCao, Zexing
dc.contributor.author曹泽星
dc.contributor.authorMo, Yirong
dc.date.accessioned2011-07-12T15:21:08Z
dc.date.available2011-07-12T15:21:08Z
dc.date.issued2006-08
dc.identifier.citationJ. Am. Chem. Soc., 2006, 128 (33):10876–10884zh_CN
dc.identifier.issn0002-7863
dc.identifier.urihttp://dx.doi.org/doi:10.1021/ja0631549
dc.identifier.urihttps://dspace.xmu.edu.cn/handle/2288/10117
dc.description.abstractMolecular dynamics ( MD) simulations have been performed at the atomic level to study the ammonium/ammonia transport across the Escherichia coli AmtB membrane protein. Although ammonia primarily exists in the form of NH4+ in aqueous solution, the recent X-ray structure determination of AmtB reveals that the ammonium/ammonia transporter proteins are ammonia-conducting channels rather than ammonium ion transporters [Khademi, S.; et al. Science 2004, 305, 1587; Zheng, L.; et al. Proc. Natl. Acad. Sci. U. S. A. 2004, 101, 17090]. Our simulations showed that the entrance of NH4+ into the periplasmic recruitment vestibule requires only 3.1 kcal/mol of energy. This is consistent with the X-ray crystal structure, where one NH4+ is captured in the binding vestibule. In this vestibule, NH4+ loses one water of hydration, but the loss is compensated by a hydrogen bond, first with the backbone carbonyl oxygen of Phe161 then with the hydroxyl group of Ser219, as well as the stabilizing pi-cation interactions with the aromatic rings of Trp148 and Phe107 in the AmtB protein. In the end of this recruitment vestibule, the phenyl ring of Phe107 dynamically switches to an open state. This is correlated with a slight rotation and shifting of the indole ring of Trp148, which eventually creates a slot for the initially buried carboxylate group of Asp160 to become exposed to the bulk solvent. A hydrogen bond wire between NH4+ and the carboxylate group of Asp160 via two water molecules was observed. Thus, Asp160 is most likely the proton acceptor from NH4+. This explains the high conservation of Asp160 in Amt proteins and why the D160A mutant would completely quench the activity of AmtB [ Javelle, A.; et al. J. Biol. Chem. 2004, 279, 8530; Marini, A. M.; et al. Curr. Genet. 2006, 49, 364]. Once NH4+ deprotonates, the phenyl ring of Phe215 rotates to open, and the subsequent passage of NH3 through the channel is straightforward.zh_CN
dc.language.isoenzh_CN
dc.publisherAMER CHEMICAL SOCzh_CN
dc.titleMolecular dynamics simulations on the Escherichia coli ammonia channel protein AmtB: Mechanism of ammonia/ammonium transportzh_CN
dc.typeArticlezh_CN


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record