Allosteric Transitions of Glutamine-Binding Protein Studied by the Elastic Network Model

Lu Jin; Nan Xiao; Chunhua Li; Jianjun Tan; Xiaoyi Zhang; Jiguo Su

doi:doi:10.11648/j.bio.20150306.14

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Allosteric Transitions of Glutamine-Binding Protein Studied by the Elastic Network Model

Lu Jin, Nan Xiao, Chunhua Li, Jianjun Tan, Xiaoyi Zhang, Jiguo Su

Published in American Journal of Bioscience and Bioengineering (Volume 3, Issue 6)

Received: 16 December 2015 Accepted: Published: 17 December 2015

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Abstract

Glutamine-Binding Protein (GlnBP) from Escherichia coli is an extremely important periplasmic binding protein. Binding of glutamine at the cleft between two domains causes a conformational change corresponding to a closure of two domains around the ligand. Because this process has a close relationship with protein function, studying this process has an important biological significance. It is very difficult for the existing experimental methods to obtain the conformational transition of GlnBP. In this paper, we studied the allosteric mechanism of GlnBP by using the adaptive Anisotropic Network Model (aANM) proposed by Bahar and obtained a relatively reasonable allosteric pathway. This work is helpful for the understanding the role of the topology structure in GlnBP conformational transition.

Published in	American Journal of Bioscience and Bioengineering (Volume 3, Issue 6)
DOI	10.11648/j.bio.20150306.14
Page(s)	162-168
Creative Commons	This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited.
Copyright	Copyright © The Author(s), 2024. Published by Science Publishing Group

Keywords

Glutamine-Binding Protein, Adaptive Anisotropic Network Model, Allosteric Mechanism

References

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APA Style

Lu Jin, Nan Xiao, Chunhua Li, Jianjun Tan, Xiaoyi Zhang, et al. (2015). Allosteric Transitions of Glutamine-Binding Protein Studied by the Elastic Network Model. American Journal of Bioscience and Bioengineering, 3(6), 162-168. https://doi.org/10.11648/j.bio.20150306.14

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ACS Style

Lu Jin; Nan Xiao; Chunhua Li; Jianjun Tan; Xiaoyi Zhang, et al. Allosteric Transitions of Glutamine-Binding Protein Studied by the Elastic Network Model. Am. J. BioSci. Bioeng. 2015, 3(6), 162-168. doi: 10.11648/j.bio.20150306.14

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AMA Style

Lu Jin, Nan Xiao, Chunhua Li, Jianjun Tan, Xiaoyi Zhang, et al. Allosteric Transitions of Glutamine-Binding Protein Studied by the Elastic Network Model. Am J BioSci Bioeng. 2015;3(6):162-168. doi: 10.11648/j.bio.20150306.14

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@article{10.11648/j.bio.20150306.14,
  author = {Lu Jin and Nan Xiao and Chunhua Li and Jianjun Tan and Xiaoyi Zhang and Jiguo Su},
  title = {Allosteric Transitions of Glutamine-Binding Protein Studied by the Elastic Network Model},
  journal = {American Journal of Bioscience and Bioengineering},
  volume = {3},
  number = {6},
  pages = {162-168},
  doi = {10.11648/j.bio.20150306.14},
  url = {https://doi.org/10.11648/j.bio.20150306.14},
  eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.bio.20150306.14},
  abstract = {Glutamine-Binding Protein (GlnBP) from Escherichia coli is an extremely important periplasmic binding protein. Binding of glutamine at the cleft between two domains causes a conformational change corresponding to a closure of two domains around the ligand. Because this process has a close relationship with protein function, studying this process has an important biological significance. It is very difficult for the existing experimental methods to obtain the conformational transition of GlnBP. In this paper, we studied the allosteric mechanism of GlnBP by using the adaptive Anisotropic Network Model (aANM) proposed by Bahar and obtained a relatively reasonable allosteric pathway. This work is helpful for the understanding the role of the topology structure in GlnBP conformational transition.},
 year = {2015}
}

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TY  - JOUR
T1  - Allosteric Transitions of Glutamine-Binding Protein Studied by the Elastic Network Model
AU  - Lu Jin
AU  - Nan Xiao
AU  - Chunhua Li
AU  - Jianjun Tan
AU  - Xiaoyi Zhang
AU  - Jiguo Su
Y1  - 2015/12/17
PY  - 2015
N1  - https://doi.org/10.11648/j.bio.20150306.14
DO  - 10.11648/j.bio.20150306.14
T2  - American Journal of Bioscience and Bioengineering
JF  - American Journal of Bioscience and Bioengineering
JO  - American Journal of Bioscience and Bioengineering
SP  - 162
EP  - 168
PB  - Science Publishing Group
SN  - 2328-5893
UR  - https://doi.org/10.11648/j.bio.20150306.14
AB  - Glutamine-Binding Protein (GlnBP) from Escherichia coli is an extremely important periplasmic binding protein. Binding of glutamine at the cleft between two domains causes a conformational change corresponding to a closure of two domains around the ligand. Because this process has a close relationship with protein function, studying this process has an important biological significance. It is very difficult for the existing experimental methods to obtain the conformational transition of GlnBP. In this paper, we studied the allosteric mechanism of GlnBP by using the adaptive Anisotropic Network Model (aANM) proposed by Bahar and obtained a relatively reasonable allosteric pathway. This work is helpful for the understanding the role of the topology structure in GlnBP conformational transition.
VL  - 3
IS  - 6
ER  -

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Author Information

Lu Jin

College of Life Science and Bioengineering, Beijing University of Technology, Beijing, China
Nan Xiao

College of Life Science and Bioengineering, Beijing University of Technology, Beijing, China
Chunhua Li

College of Life Science and Bioengineering, Beijing University of Technology, Beijing, China
Jianjun Tan

College of Life Science and Bioengineering, Beijing University of Technology, Beijing, China
Xiaoyi Zhang

College of Life Science and Bioengineering, Beijing University of Technology, Beijing, China
Jiguo Su

College of Science, Yanshan University, Qinhuangdao, China

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Plain Text BibTeX RIS

APA Style

Lu Jin, Nan Xiao, Chunhua Li, Jianjun Tan, Xiaoyi Zhang, et al. (2015). Allosteric Transitions of Glutamine-Binding Protein Studied by the Elastic Network Model. American Journal of Bioscience and Bioengineering, 3(6), 162-168. https://doi.org/10.11648/j.bio.20150306.14

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ACS Style

Lu Jin; Nan Xiao; Chunhua Li; Jianjun Tan; Xiaoyi Zhang, et al. Allosteric Transitions of Glutamine-Binding Protein Studied by the Elastic Network Model. Am. J. BioSci. Bioeng. 2015, 3(6), 162-168. doi: 10.11648/j.bio.20150306.14

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AMA Style

Lu Jin, Nan Xiao, Chunhua Li, Jianjun Tan, Xiaoyi Zhang, et al. Allosteric Transitions of Glutamine-Binding Protein Studied by the Elastic Network Model. Am J BioSci Bioeng. 2015;3(6):162-168. doi: 10.11648/j.bio.20150306.14

Copy | Download

@article{10.11648/j.bio.20150306.14,
  author = {Lu Jin and Nan Xiao and Chunhua Li and Jianjun Tan and Xiaoyi Zhang and Jiguo Su},
  title = {Allosteric Transitions of Glutamine-Binding Protein Studied by the Elastic Network Model},
  journal = {American Journal of Bioscience and Bioengineering},
  volume = {3},
  number = {6},
  pages = {162-168},
  doi = {10.11648/j.bio.20150306.14},
  url = {https://doi.org/10.11648/j.bio.20150306.14},
  eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.bio.20150306.14},
  abstract = {Glutamine-Binding Protein (GlnBP) from Escherichia coli is an extremely important periplasmic binding protein. Binding of glutamine at the cleft between two domains causes a conformational change corresponding to a closure of two domains around the ligand. Because this process has a close relationship with protein function, studying this process has an important biological significance. It is very difficult for the existing experimental methods to obtain the conformational transition of GlnBP. In this paper, we studied the allosteric mechanism of GlnBP by using the adaptive Anisotropic Network Model (aANM) proposed by Bahar and obtained a relatively reasonable allosteric pathway. This work is helpful for the understanding the role of the topology structure in GlnBP conformational transition.},
 year = {2015}
}

Copy | Download

TY  - JOUR
T1  - Allosteric Transitions of Glutamine-Binding Protein Studied by the Elastic Network Model
AU  - Lu Jin
AU  - Nan Xiao
AU  - Chunhua Li
AU  - Jianjun Tan
AU  - Xiaoyi Zhang
AU  - Jiguo Su
Y1  - 2015/12/17
PY  - 2015
N1  - https://doi.org/10.11648/j.bio.20150306.14
DO  - 10.11648/j.bio.20150306.14
T2  - American Journal of Bioscience and Bioengineering
JF  - American Journal of Bioscience and Bioengineering
JO  - American Journal of Bioscience and Bioengineering
SP  - 162
EP  - 168
PB  - Science Publishing Group
SN  - 2328-5893
UR  - https://doi.org/10.11648/j.bio.20150306.14
AB  - Glutamine-Binding Protein (GlnBP) from Escherichia coli is an extremely important periplasmic binding protein. Binding of glutamine at the cleft between two domains causes a conformational change corresponding to a closure of two domains around the ligand. Because this process has a close relationship with protein function, studying this process has an important biological significance. It is very difficult for the existing experimental methods to obtain the conformational transition of GlnBP. In this paper, we studied the allosteric mechanism of GlnBP by using the adaptive Anisotropic Network Model (aANM) proposed by Bahar and obtained a relatively reasonable allosteric pathway. This work is helpful for the understanding the role of the topology structure in GlnBP conformational transition.
VL  - 3
IS  - 6
ER  -

Copy | Download