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dc.contributor.authorLaulumaa, Saaraen_US
dc.contributor.authorKursula, Petrien_US
dc.date.accessioned2019-12-17T12:54:45Z
dc.date.available2019-12-17T12:54:45Z
dc.date.issued2019-08-22
dc.PublishedLaulumaa S, Kursula P. Sub-atomic resolution crystal structures reveal conserved geometric outliers at functional sites. Molecules. 2019;24:3044eng
dc.identifier.issn1420-3049
dc.identifier.urihttps://hdl.handle.net/1956/21162
dc.description.abstractMyelin protein 2 (P2) is a peripheral membrane protein of the vertebrate nervous system myelin sheath, having possible roles in both lipid transport and 3D molecular organization of the multilayered myelin membrane. We extended our earlier crystallographic studies on human P2 and refined its crystal structure at an ultrahigh resolution of 0.72 Å in perdeuterated form and 0.86 Å in hydrogenated form. Characteristic differences in C–H…O hydrogen bond patterns were observed between extended β strands, kinked or ending strands, and helices. Often, side-chain C–H groups engage in hydrogen bonding with backbone carbonyl moieties. The data highlight several amino acid residues with unconventional conformations, including both bent aromatic rings and twisted guanidinium groups on arginine side chains, as well as non-planar peptide bonds. In two locations, such non-ideal conformations cluster, providing proof of local functional strain. Other ultrahigh-resolution protein structures similarly contain chemical groups, which break planarity rules. For example, in Src homology 3 (SH3) domains, a conserved bent aromatic residue is observed near the ligand binding site. Fatty acid binding protein (FABP) 3, belonging to the same family as P2, has several side chains and peptide bonds bent exactly as those in P2. We provide a high-resolution snapshot on non-ideal conformations of amino acid residues under local strain, possibly relevant to biological function. Geometric outliers observed in ultrahigh-resolution protein structures are real and likely relevant for ligand binding and conformational changes. Furthermore, the deuteration of protein and/or solvent are promising variables in protein crystal optimization.en_US
dc.language.isoengeng
dc.publisherMDPIeng
dc.rightsAttribution CC BYeng
dc.rights.urihttp://creativecommons.org/licenses/by/4.0eng
dc.subjectultrahigh resolutioneng
dc.subjectprotein structureeng
dc.subjectmyelin proteineng
dc.subjectfatty acid-binding proteineng
dc.subjectgeometryeng
dc.subjectdeuterationeng
dc.titleSub-atomic resolution crystal structures reveal conserved geometric outliers at functional sitesen_US
dc.typePeer reviewed
dc.typeJournal article
dc.date.updated2019-10-23T08:37:45Z
dc.description.versionpublishedVersionen_US
dc.rights.holderCopyright 2019 The Author(s)
dc.identifier.doihttps://doi.org/10.3390/molecules24173044
dc.identifier.cristin1738396
dc.source.journalMolecules


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