Sökning: onr:"swepub:oai:lup.lub.lu.se:ab29dbe9-db8b-4aaf-8694-6d671b498a1a" > Structure and Dynam...
Fältnamn | Indikatorer | Metadata |
---|---|---|
000 | 03173naa a2200505 4500 | |
001 | oai:lup.lub.lu.se:ab29dbe9-db8b-4aaf-8694-6d671b498a1a | |
003 | SwePub | |
008 | 160401s2014 | |||||||||||000 ||eng| | |
024 | 7 | a https://lup.lub.lu.se/record/45927722 URI |
024 | 7 | a https://doi.org/10.1016/j.bpj.2014.06.0132 DOI |
040 | a (SwePub)lu | |
041 | a engb eng | |
042 | 9 SwePub | |
072 | 7 | a art2 swepub-publicationtype |
072 | 7 | a ref2 swepub-contenttype |
100 | 1 | a Hong, Liang4 aut |
245 | 1 0 | a Structure and Dynamics of a Compact State of a Multidomain Protein, the Mercuric Ion Reductase |
264 | 1 | b Elsevier BV,c 2014 |
520 | a 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. | |
650 | 7 | a NATURVETENSKAPx Biologix Biofysik0 (SwePub)106032 hsv//swe |
650 | 7 | a NATURAL SCIENCESx Biological Sciencesx Biophysics0 (SwePub)106032 hsv//eng |
700 | 1 | a Sharp, Melissau Lund University,Lunds universitet,European Spallation Source ESS AB,Stiftelser och övriga anknutna verksamheter,Other Institutions and Utilities4 aut0 (Swepub:lu)esss-mss |
700 | 1 | a Poblete, Simon4 aut |
700 | 1 | a Bieh, Ralf4 aut |
700 | 1 | a Zamponi, Michaele4 aut |
700 | 1 | a Szekely, Noemi4 aut |
700 | 1 | a Appavou, Marie-Sousai4 aut |
700 | 1 | a Winkler, Roland G.4 aut |
700 | 1 | a Nauss, Rachel E.4 aut |
700 | 1 | a Johs, Alexander4 aut |
700 | 1 | a Parks, Jerry M.4 aut |
700 | 1 | a Yi, Zheng4 aut |
700 | 1 | a Cheng, Xiaolin4 aut |
700 | 1 | a Liang, Liyuan4 aut |
700 | 1 | a Ohl, Michael4 aut |
700 | 1 | a Miller, Susan M.4 aut |
700 | 1 | a Richter, Dieter4 aut |
700 | 1 | a Gompper, Gerhard4 aut |
700 | 1 | a Smith, Jeremy C.4 aut |
710 | 2 | a European Spallation Source ESS ABb Stiftelser och övriga anknutna verksamheter4 org |
773 | 0 | t Biophysical Journald : Elsevier BVg 107:2, s. 393-400q 107:2<393-400x 1542-0086x 0006-3495 |
856 | 4 | u http://dx.doi.org/10.1016/j.bpj.2014.06.013y FULLTEXT |
856 | 4 | u http://www.cell.com/article/S0006349514006201/pdf |
856 | 4 8 | u https://lup.lub.lu.se/record/4592772 |
856 | 4 8 | u https://doi.org/10.1016/j.bpj.2014.06.013 |
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