This title appears in the Scientific Report :
2014
Please use the identifier:
http://dx.doi.org/10.1016/j.bpj.2014.06.013 in citations.
Structure and Dynamics of a Compact State of a Multidomain Protein, the Mercuric Ion Reductase
Structure and Dynamics of a Compact State of a Multidomain Protein, the Mercuric Ion Reductase
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 complement...
Saved in:
Personal Name(s): | Hong, Liang (Corresponding Author) |
---|---|
Sharp, Melissa  / Poblete, Simón / Biehl, Ralf / Zamponi, Michaela / Szekely, Noemi / Appavou, Marie-Sousai / Winkler, Roland G. / Nauss, Rachel E. / Johs, Alexander / Parks, Jerry  / Yi, Zheng / Cheng, Xiaolin / Liang, Liyuan / Ohl, Michael / Miller, Susan  / Richter, Dieter / Gompper, Gerhard / Smith, Jeremy  | |
Contributing Institute: |
Theorie der Weichen Materie und Biophysik; ICS-2 JCNS-FRM-II; JCNS-FRM-II Neutronenstreuung; JCNS-1 Neutronenstreuung; ICS-1 JCNS-SNS; JCNS-SNS Theorie der Weichen Materie und Biophysik; IAS-2 |
Published in: | Biophysical journal, 107 (2014) 2, S. 393 - 400 |
Imprint: |
New York, NY
Rockefeller Univ. Press
2014
|
DOI: |
10.1016/j.bpj.2014.06.013 |
PubMed ID: |
25028881 |
Document Type: |
Journal Article |
Research Program: |
JCNS Soft Matter Composites |
Subject (ZB): | |
Publikationsportal JuSER |
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. |