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Molecular dynamics simulations on the mechanism of transporting methylamine and ammonia by ammonium transporter AmtB

AmtB is one of the ammonium transporter proteins facilitating the ammonium transport across the cellular membranes. Experimentally, the substrate used in in vitro studies is the radio labeled [(14)C]methylammonium, rather than ammonium itself. To explore the similarity and difference of the conducti... Full description

Journal Title: The journal of physical chemistry. B 25 November 2010, Vol.114(46), pp.15172-9
Main Author: Wang, Jinan
Other Authors: Yang, Huaiyu , Zuo, Zhili , Yan, Xiuhua , Wang, Yong , Luo, Xiaomin , Jiang, Hualiang , Chen, Kaixian , Zhu, Weiliang
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: E-ISSN: 1520-5207 ; PMID: 20973592 Version:1 ; DOI: 10.1021/jp104508k
Link: http://pubmed.gov/20973592
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recordid: medline20973592
title: Molecular dynamics simulations on the mechanism of transporting methylamine and ammonia by ammonium transporter AmtB
format: Article
creator:
  • Wang, Jinan
  • Yang, Huaiyu
  • Zuo, Zhili
  • Yan, Xiuhua
  • Wang, Yong
  • Luo, Xiaomin
  • Jiang, Hualiang
  • Chen, Kaixian
  • Zhu, Weiliang
subjects:
  • Ammonia -- Metabolism
  • Cation Transport Proteins -- Metabolism
  • Escherichia Coli Proteins -- Metabolism
  • Methylamines -- Metabolism
ispartof: The journal of physical chemistry. B, 25 November 2010, Vol.114(46), pp.15172-9
description: AmtB is one of the ammonium transporter proteins facilitating the ammonium transport across the cellular membranes. Experimentally, the substrate used in in vitro studies is the radio labeled [(14)C]methylammonium, rather than ammonium itself. To explore the similarity and difference of the conduction mechanism of methylamine and ammonia molecules through AmtB, molecular dynamics simulations on 22 carefully designed systems were performed, which demonstrated that methylamine could be automatically transported in a very similar way to ammonia. The driving force for the conduction is mainly the hydrogen bond network comprising His168, His318, and Tyr32, working in coordination with NH-π interaction with residue Trp212. Then, Ser263 translocated the substrates from the exit gate into the cytoplasm by hydrogen bond interaction. The aromatic ring of Trp212 acted like a springboard to facilitate the translocation of the substrates from site Am2 to Am4 via NH-π interaction. Without the mediation...
language: eng
source:
identifier: E-ISSN: 1520-5207 ; PMID: 20973592 Version:1 ; DOI: 10.1021/jp104508k
fulltext: fulltext
issn:
  • 15205207
  • 1520-5207
url: Link


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titleMolecular dynamics simulations on the mechanism of transporting methylamine and ammonia by ammonium transporter AmtB
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subjectAmmonia -- Metabolism ; Cation Transport Proteins -- Metabolism ; Escherichia Coli Proteins -- Metabolism ; Methylamines -- Metabolism
descriptionAmtB is one of the ammonium transporter proteins facilitating the ammonium transport across the cellular membranes. Experimentally, the substrate used in in vitro studies is the radio labeled [(14)C]methylammonium, rather than ammonium itself. To explore the similarity and difference of the conduction mechanism of methylamine and ammonia molecules through AmtB, molecular dynamics simulations on 22 carefully designed systems were performed, which demonstrated that methylamine could be automatically transported in a very similar way to ammonia. The driving force for the conduction is mainly the hydrogen bond network comprising His168, His318, and Tyr32, working in coordination with NH-π interaction with residue Trp212. Then, Ser263 translocated the substrates from the exit gate into the cytoplasm by hydrogen bond interaction. The aromatic ring of Trp212 acted like a springboard to facilitate the translocation of the substrates from site Am2 to Am4 via NH-π interaction. Without the mediation...
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descriptionAmtB is one of the ammonium transporter proteins facilitating the ammonium transport across the cellular membranes. Experimentally, the substrate used in in vitro studies is the radio labeled [(14)C]methylammonium, rather than ammonium itself. To explore the similarity and difference of the conduction mechanism of methylamine and ammonia molecules through AmtB, molecular dynamics simulations on 22 carefully designed systems were performed, which demonstrated that methylamine could be automatically transported in a very similar way to ammonia. The driving force for the conduction is mainly the hydrogen bond network comprising His168, His318, and Tyr32, working in coordination with NH-π interaction with residue Trp212. Then, Ser263 translocated the substrates from the exit gate into the cytoplasm by hydrogen bond interaction. The aromatic ring of Trp212 acted like a springboard to facilitate the translocation of the substrates from site Am2 to Am4 via NH-π interaction. Without the mediation...
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abstractAmtB is one of the ammonium transporter proteins facilitating the ammonium transport across the cellular membranes. Experimentally, the substrate used in in vitro studies is the radio labeled [(14)C]methylammonium, rather than ammonium itself. To explore the similarity and difference of the conduction mechanism of methylamine and ammonia molecules through AmtB, molecular dynamics simulations on 22 carefully designed systems were performed, which demonstrated that methylamine could be automatically transported in a very similar way to ammonia. The driving force for the conduction is mainly the hydrogen bond network comprising His168, His318, and Tyr32, working in coordination with NH-π interaction with residue Trp212. Then, Ser263 translocated the substrates from the exit gate into the cytoplasm by hydrogen bond interaction. The aromatic ring of Trp212 acted like a springboard to facilitate the translocation of the substrates from site Am2 to Am4 via NH-π interaction. Without the mediation...
doi10.1021/jp104508k
pmid20973592
date2010-11-25