دورية أكاديمية
Mapping periplasmic binding protein oligosaccharide recognition with neutron crystallography.
| العنوان: | Mapping periplasmic binding protein oligosaccharide recognition with neutron crystallography. |
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| المؤلفون: | Shukla S; Neutron Scattering Division, Oak Ridge National Laboratory, Oak Ridge, TN, 37831, USA.; UT-ORNL Graduate School in Genome Science and Technology, The University of Tennessee at Knoxville, Knoxville, TN, 37966, USA.; Department of Microbiology and Immunology, Northwestern University, Chicago, IL, 60611, USA., Myles DA; Neutron Scattering Division, Oak Ridge National Laboratory, Oak Ridge, TN, 37831, USA. mylesda@ornl.gov., Cuneo MJ; Neutron Scattering Division, Oak Ridge National Laboratory, Oak Ridge, TN, 37831, USA. matt.cuneo@stjude.org.; Department of Structural Biology, St. Jude Children's Research Hospital, Memphis, TN, 38105, USA. matt.cuneo@stjude.org. |
| المصدر: | Scientific reports [Sci Rep] 2022 Oct 21; Vol. 12 (1), pp. 17647. Date of Electronic Publication: 2022 Oct 21. |
| نوع المنشور: | Journal Article; Research Support, U.S. Gov't, Non-P.H.S. |
| اللغة: | English |
| بيانات الدورية: | Publisher: Nature Publishing Group Country of Publication: England NLM ID: 101563288 Publication Model: Electronic Cited Medium: Internet ISSN: 2045-2322 (Electronic) Linking ISSN: 20452322 NLM ISO Abbreviation: Sci Rep Subsets: MEDLINE |
| أسماء مطبوعة: | Original Publication: London : Nature Publishing Group, copyright 2011- |
| مواضيع طبية MeSH: | Periplasmic Binding Proteins*/metabolism, Protein Conformation ; Crystallography, X-Ray ; Models, Molecular ; Binding Sites ; Hydrogen Bonding ; Oligosaccharides/chemistry ; Neutrons ; Sugars ; Water/metabolism ; Hydrogen/metabolism ; Protein Binding |
| مستخلص: | Numerous studies have shown how periplasmic binding proteins (PBPs) bind substrates with exquisite specificity, even distinguishing between sugar epimers and anomers, or structurally similar ions. Yet, marked substrate promiscuity is also a feature encoded in some PBPs. Except for three sub-Ångström crystal structures, there are no reports of hydrogen atom positions in the remaining (> 1000) PBP structures. The previous X-ray crystal structure of the maltodextrin periplasmic-binding protein from Thermotoga maritima (tmMBP) complexed with oligosaccharide showed a large network of interconnected water molecules stretching from one end of the substrate binding pocket to the other. These water molecules are positioned to form multiple hydrogen bonds, as well as forming interactions between the protein and substrate. Here we present the neutron crystal structure of tmMBP to a resolution of 2.1 Å. This is the first neutron crystal structure from the PBP superfamily and here we unambiguously identify the nature and orientation of the hydrogen bonding and water-mediated interactions involved in stabilizing a tetrasaccharide in the binding site. More broadly, these results demonstrate the conserved intricate mechanisms that underlie substrate-specificity and affinity in PBPs. (© 2022. UT-Battelle, LLC.) |
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| المشرفين على المادة: | 0 (Periplasmic Binding Proteins) 0 (Oligosaccharides) 0 (Sugars) 059QF0KO0R (Water) 7YNJ3PO35Z (Hydrogen) |
| تواريخ الأحداث: | Date Created: 20221021 Date Completed: 20221025 Latest Revision: 20230117 |
| رمز التحديث: | 20240829 |
| مُعرف محوري في PubMed: | PMC9587032 |
| DOI: | 10.1038/s41598-022-20542-8 |
| PMID: | 36271099 |
| قاعدة البيانات: | MEDLINE |
Find this article in full text from Springer Verlag. 
Full Text Finder | تدمد: | 2045-2322 |
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| DOI: | 10.1038/s41598-022-20542-8 |