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It\u2019s widely distributed in both Gram-negative and Gram-positive bacteria but with barely detectable sequence identities between the two sources. To provide structural basis for the considerable biochemical and biophysical experiments previously performed on\n                    <jats:italic>Tn501<\/jats:italic>\n                    and\n                    <jats:italic>Tn21<\/jats:italic>\n                    MerR from Gram-negative bacteria, we analyzed the crystal structure of mercury(II)\n                    <jats:italic>-<\/jats:italic>\n                    bound\n                    <jats:italic>Tn501<\/jats:italic>\n                    MerR. The structure in the metal-binding domain provides\n                    <jats:italic>Tn501<\/jats:italic>\n                    MerR with a high affinity for mercury(II) and the ability to distinguish mercury(II) from other metals with its unique planar trigonal coordination geometry, which is adopted by both Gram-negative and Gram-positive bacteria. The mercury(II) coordination state in the C-terminal metal-binding domain is transmitted through the allosteric network across the dimer interface to the N-terminal DNA-binding domain. Together with the previous mutagenesis analyses, the present data indicate that the residues in the allosteric pathway have a central role in maintaining the functions of\n                    <jats:italic>Tn501<\/jats:italic>\n                    MerR. In addition, the complex structure exhibits significant differences in tertiary and quaternary structural arrangements compared to those of\n                    <jats:italic>Bacillus<\/jats:italic>\n                    MerR from Gram-positive bacteria, which probably enable them to function with specific promoter DNA with different spacers between \u221235 and \u221210 elements.\n                  <\/jats:p>","DOI":"10.1038\/srep33391","type":"journal-article","created":{"date-parts":[[2016,9,19]],"date-time":"2016-09-19T06:04:22Z","timestamp":1474265062000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":44,"title":["Structural Analysis of the Hg(II)-Regulatory Protein Tn501 MerR from Pseudomonas aeruginosa"],"prefix":"10.1038","volume":"6","author":[{"given":"Dan","family":"Wang","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shanqing","family":"Huang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pingying","family":"Liu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xichun","family":"Liu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yafeng","family":"He","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Weizhong","family":"Chen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Qingyuan","family":"Hu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tianbiao","family":"Wei","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jianhua","family":"Gan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jing","family":"Ma","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hao","family":"Chen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2016,9,19]]},"reference":[{"key":"BFsrep33391_CR1","doi-asserted-by":"publisher","first-page":"149","DOI":"10.1002\/tox.10116","volume":"18","author":"PB Tchounwou","year":"2003","unstructured":"Tchounwou, P. 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