Please use this identifier to cite or link to this item:
http://hdl.handle.net/10397/65705
DC Field | Value | Language |
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dc.contributor | Department of Applied Biology and Chemical Technology | - |
dc.creator | Hu, M | - |
dc.creator | Guo, J | - |
dc.creator | Cheng, Q | - |
dc.creator | Yang, Z | - |
dc.creator | Chan, EWC | - |
dc.creator | Chen, S | - |
dc.creator | Hao, Q | - |
dc.date.accessioned | 2017-05-22T02:09:05Z | - |
dc.date.available | 2017-05-22T02:09:05Z | - |
dc.identifier.uri | http://hdl.handle.net/10397/65705 | - |
dc.language.iso | en | en_US |
dc.publisher | Nature Publishing Group | en_US |
dc.rights | This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ | en_US |
dc.rights | © The Author(s) 2016 | en_US |
dc.rights | The following publication Hu, M. et al. Crystal Structure of Escherichia coli originated MCR-1, a phosphoethanolamine transferase for Colistin Resistance. Sci. Rep. 6, 38793 (2016) is available at https://dx.doi.org/10.1038/srep38793 | en_US |
dc.title | Crystal structure of Escherichia coli originated MCR-1, a phosphoethanolamine transferase for colistin resistance | en_US |
dc.type | Journal/Magazine Article | en_US |
dc.identifier.volume | 6 | - |
dc.identifier.doi | 10.1038/srep38793 | - |
dcterms.abstract | MCR-1 is a phosphoethanolamine (pEtN) transferase that modifies the pEtN moiety of lipid A, conferring resistance to colistin, which is an antibiotic belonging to the class of polypeptide antibiotics known as polymyxins and is the last-line antibiotic used to treat multidrug resistant bacterial infections. Here we determined the crystal structure of the catalytic domain of MCR-1 (MCR-1-ED), which is originated in Escherichia coli (E. coli). MCR-1-ED was found to comprise several classical β-α-β-α motifs that constitute a "sandwich" conformation. Two interlaced molecules with different phosphorylation status of the residue T285 could give rise to two functional statuses of MCR-1 depending on the physiological conditions. MCR-1, like other known pEtN transferases, possesses an enzymatic site equipped with zinc binding residues. Interestingly, two zinc ions were found to mediate intermolecular interactions between MCR-1-ED molecules in one asymmetric unit and hence concatenation of MCR-1, allowing the protein to be oligomer. Findings of this work shall provide important insight into development of effective and clinically useful inhibitors of MCR-1 or structurally similar enzymes. | - |
dcterms.accessRights | open access | en_US |
dcterms.bibliographicCitation | Scientific reports, 13 2016, v. 6, no. , 38793, p. 1-7 | - |
dcterms.isPartOf | Scientific reports | - |
dcterms.issued | 2016 | - |
dc.identifier.isi | WOS:000389673000001 | - |
dc.identifier.scopus | 2-s2.0-85005963667 | - |
dc.identifier.eissn | 2045-2322 | - |
dc.identifier.artn | 38793 | - |
dc.description.oa | Version of Record | en_US |
dc.identifier.FolderNumber | OA_IR/PIRA | en_US |
dc.description.pubStatus | Published | en_US |
dc.description.oaCategory | CC | en_US |
Appears in Collections: | Journal/Magazine Article |
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File | Description | Size | Format | |
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Hu_Crystal_Structure_Escherichia.pdf | 2.23 MB | Adobe PDF | View/Open |
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