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Substrate recognition and transport behavior analyses of amino acid antiporter with coarse-grained models

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Molecular BioSystems Vol - 6 Issue - 9

Molecular BioSystems Vol - 6 Issue - 8

Molecular BioSystems Vol - 6 Issue - 7

Molecular BioSystems Vol - 6 Issue - 6

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Molecular BioSystems Vol - 6 Issue - 4

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Substrate recognition and transport behavior analyses of amino acid antiporter with coarse-grained models

Content Provider	Royal Society of Chemistry (RSC)
Author	Jiao, Xiong Hu, Jian-ping Chang, Shan Tian, Xu-hong Lin, Pi-yuan
Copyright Year	2010
Abstract	The L-arginine (Arg)/agmatine (Agm) antiporter AdiC is a vital transport protein of the arginine-dependent extreme acid resistance system of enteric bacteria. Recently, both substrate-free and Arg-bound structures of AdiC were determined by X-ray crystallography. In this article, the two different proteins were investigated with three simple models. Gaussian network model provided the information of conformational changes. It is found that Arg binding induces structural rearrangement in the extracellular domain, and transmembrane helix 6 (TM6) has the most pronounced trend of conformational changes. The moving directions of fluctuation regions were further ascertained by using anisotropy elastic network model and cross-correlation analysis. Interestingly, the two substrate-binding sites hypothesis of AdiC was confirmed directly by molecular docking. Furthermore, the binding preferences of these two sites were explained from the aspects of electrostatic complementarity and geometric matching. These simple coarse-grained analyses can be used as a general and quick method for the mechanism studies of transport proteins.
Starting Page	2430
Ending Page	2438
Page Count	9
File Format	HTM / HTML PDF
ISSN	1742206X
Volume Number	6
Issue Number	12
Journal	Molecular BioSystems
DOI	10.1039/c005266c
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	X-ray crystallography Arginine Antiporter Anisotropy Annual general meeting Docking (molecular) Gaussian network model Bacteria Agmatine Protein Cross-correlation
Content Type	Text
Resource Type	Article
Subject	Molecular Biology Biotechnology

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Molecular mechanism of pH-dependent substrate transport by an arginine-agmatine antiporter.

Arginine oscillation explains $Na^{+}$ independence in the substrate/product antiporter CaiT

Molecular mechanism of pH-dependent substrate transport by an arginine-agmatine antiporter

Molecular mechanism of substrate selectivity of the arginine-agmatine Antiporter AdiC

Protonation of Glutamate 208 Induces the Release of Agmatine in an Outward-facing Conformation of an Arginine/Agmatine Antiporter

Molecular basis of substrate-induced permeation by an amino acid antiporter.

Arginine-agmatine antiporter in extreme acid resistance in Escherichia coli.

YjdE (AdiC) is the arginine:agmatine antiporter essential for arginine-dependent acid resistance in Escherichia coli (2003)

Escherichia coli Acid Resistance in Antiporter Essential for Arginine-Dependent YjdE ( AdiC ) Is the Arginine : Agmatine

Substrate recognition and transport behavior analyses of amino acid antiporter with coarse-grained models

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Substrate recognition and transport behavior analyses of amino acid antiporter with coarse-grained models