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Structure and Dynamics of a Compact State of a Multidomain Protein, the Mercuric Ion Reductase

Hong, Liang; Sharp, Melissa LU ; Poblete, Simon; Bieh, Ralf; Zamponi, Michaele; Szekely, Noemi; Appavou, Marie-Sousai; Winkler, Roland G.; Nauss, Rachel E. and Johs, Alexander, et al. (2014) In Biophysical Journal 107(2). p.393-400
Abstract
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... (More)
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. (Less)
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publication status
published
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Biophysical Journal
volume
107
issue
2
pages
393 - 400
publisher
Cell Press
external identifiers
  • wos:000339148500015
  • scopus:84904563281
ISSN
1542-0086
DOI
10.1016/j.bpj.2014.06.013
language
English
LU publication?
yes
id
ab29dbe9-db8b-4aaf-8694-6d671b498a1a (old id 4592772)
date added to LUP
2014-09-03 11:24:54
date last changed
2017-05-28 03:27:53
@article{ab29dbe9-db8b-4aaf-8694-6d671b498a1a,
  abstract     = {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.},
  author       = {Hong, Liang and Sharp, Melissa and Poblete, Simon and Bieh, Ralf and Zamponi, Michaele 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.},
  issn         = {1542-0086},
  language     = {eng},
  number       = {2},
  pages        = {393--400},
  publisher    = {Cell Press},
  series       = {Biophysical Journal},
  title        = {Structure and Dynamics of a Compact State of a Multidomain Protein, the Mercuric Ion Reductase},
  url          = {http://dx.doi.org/10.1016/j.bpj.2014.06.013},
  volume       = {107},
  year         = {2014},
}