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Title: Structure and dynamics of a compact state of a multidomain protein, the mercuric ion reductase

Abstract

Here, the functional efficacy of colocalized, linked protein domains is dependent on linker flexibility and system compaction. However, the detailed characterization of these properties in aqueous solution presents an enduring challenge. Here, we employ a novel, to our knowledge, combination of complementary techniques, including small-angle neutron scattering, neutron spin-echo spectroscopy, and all-atom molecular dynamics and coarse-grained simulation, to identify and characterize in detail the structure and dynamics of a compact form of mercuric ion reductase (MerA), an enzyme central to bacterial mercury resistance. MerA possesses metallochaperone-like N-terminal domains (NmerA) tethered to its catalytic core domain by linkers. The NmerA domains are found to interact principally through electrostatic interactions with the core, leashed by the linkers so as to subdiffuse on the surface over an area close to the core C-terminal Hg(II)-binding cysteines. How this compact, dynamical arrangement may facilitate delivery of Hg(II) from NmerA to the core domain is discussed.

Authors:
 [1];  [2];  [3];  [3];  [4];  [4];  [4];  [3];  [5];  [6];  [6];  [7];  [6];  [6];  [8];  [5];  [3];  [3];  [7]
  1. Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States); Univ. of Tennessee, Knoxville, TN (United States); Shanghai Jiao Tong Univ., Shanghai (China)
  2. European Spallation Source ESS AB, Lund (Sweden); Outstation at the Spallation Neutron Source (SNS), Oak Ridge, TN (United States)
  3. Forschungszentrum Julich, Julich (Germany)
  4. Julich Centre for Neutron Science (JCNS), Garching (Germany)
  5. Univ. of California, San Francisco, CA (United States)
  6. Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
  7. Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States); Univ. of Tennessee, Knoxville, TN (United States)
  8. Julich Center for Neutron Science (JCNS), Garching (Germany)
Publication Date:
Research Org.:
Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
Sponsoring Org.:
USDOE Office of Science (SC)
OSTI Identifier:
1265923
DOE Contract Number:  
AC05-00OR22725
Resource Type:
Journal Article
Resource Relation:
Journal Name: Biophysical Journal; Journal Volume: 107; Journal Issue: 2
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES

Citation Formats

Hong, Liang, Sharp, Melissa A., Poblete, Simon, Biehle, Ralf, Zamponi, Michaela, Szekely, Noemi, Appavou, Marie -Sousai, Winkler, Roland G., Nauss, Rachel E., Johs, Alexander, Parks, Jerry M., Yi, Zheng, Cheng, Xiaolin, Liang, Liyuan, Ohl, Michael, Miller, Susan M., Richter, Dieter, Gompper, Gerhard, and Smith, Jeremy C.. Structure and dynamics of a compact state of a multidomain protein, the mercuric ion reductase. United States: N. p., 2014. Web. doi:10.1016/j.bpj.2014.06.013.
Hong, Liang, Sharp, Melissa A., Poblete, Simon, Biehle, Ralf, Zamponi, Michaela, Szekely, Noemi, Appavou, Marie -Sousai, Winkler, Roland G., Nauss, Rachel E., Johs, Alexander, Parks, Jerry M., Yi, Zheng, Cheng, Xiaolin, Liang, Liyuan, Ohl, Michael, Miller, Susan M., Richter, Dieter, Gompper, Gerhard, & Smith, Jeremy C.. Structure and dynamics of a compact state of a multidomain protein, the mercuric ion reductase. United States. doi:10.1016/j.bpj.2014.06.013.
Hong, Liang, Sharp, Melissa A., Poblete, Simon, Biehle, Ralf, Zamponi, Michaela, Szekely, Noemi, Appavou, Marie -Sousai, Winkler, Roland G., Nauss, Rachel E., Johs, Alexander, Parks, Jerry M., Yi, Zheng, Cheng, Xiaolin, Liang, Liyuan, Ohl, Michael, Miller, Susan M., Richter, Dieter, Gompper, Gerhard, and Smith, Jeremy C.. Tue . "Structure and dynamics of a compact state of a multidomain protein, the mercuric ion reductase". United States. doi:10.1016/j.bpj.2014.06.013.
@article{osti_1265923,
title = {Structure and dynamics of a compact state of a multidomain protein, the mercuric ion reductase},
author = {Hong, Liang and Sharp, Melissa A. and Poblete, Simon and Biehle, Ralf and Zamponi, Michaela and Szekely, Noemi and Appavou, Marie -Sousai and Winkler, Roland G. and Nauss, Rachel E. and Johs, Alexander and Parks, Jerry M. and Yi, Zheng and Cheng, Xiaolin and Liang, Liyuan and Ohl, Michael and Miller, Susan M. and Richter, Dieter and Gompper, Gerhard and Smith, Jeremy C.},
abstractNote = {Here, the functional efficacy of colocalized, linked protein domains is dependent on linker flexibility and system compaction. However, the detailed characterization of these properties in aqueous solution presents an enduring challenge. Here, we employ a novel, to our knowledge, combination of complementary techniques, including small-angle neutron scattering, neutron spin-echo spectroscopy, and all-atom molecular dynamics and coarse-grained simulation, to identify and characterize in detail the structure and dynamics of a compact form of mercuric ion reductase (MerA), an enzyme central to bacterial mercury resistance. MerA possesses metallochaperone-like N-terminal domains (NmerA) tethered to its catalytic core domain by linkers. The NmerA domains are found to interact principally through electrostatic interactions with the core, leashed by the linkers so as to subdiffuse on the surface over an area close to the core C-terminal Hg(II)-binding cysteines. How this compact, dynamical arrangement may facilitate delivery of Hg(II) from NmerA to the core domain is discussed.},
doi = {10.1016/j.bpj.2014.06.013},
journal = {Biophysical Journal},
number = 2,
volume = 107,
place = {United States},
year = {Tue Jul 15 00:00:00 EDT 2014},
month = {Tue Jul 15 00:00:00 EDT 2014}
}