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Modeled 3D-Structur...
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Linares-Pastén, Javier A.Lund University,Lunds universitet,Bioteknik,Centrum för tillämpade biovetenskaper,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biotechnology,Center for Applied Life Sciences,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
(författare)
Modeled 3D-Structures of Proteobacterial Transglycosylases from Glycoside Hydrolase Family 17 Give Insight in Ligand Interactions Explaining Differences in Transglycosylation Products
- Artikel/kapitelEngelska2021
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LIBRIS-ID:oai:lup.lub.lu.se:b1efa33f-7a6a-48d4-8652-526545762b58
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https://lup.lub.lu.se/record/b1efa33f-7a6a-48d4-8652-526545762b58URI
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https://doi.org/10.3390/app11094048DOI
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Språk:engelska
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Sammanfattning på:engelska
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Ämneskategori:art swepub-publicationtype
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Ämneskategori:ref swepub-contenttype
Anmärkningar
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The structures of glycoside hydrolase family 17 (GH17) catalytic modules from modular proteins in the ndvB loci in Pseudomonas aeruginosa (Glt1), P. putida (Glt3) and Bradyrhizobium diazoefficiens (previously B. japonicum) (Glt20) were modeled to shed light on reported differences between these homologous transglycosylases concerning substrate size, preferred cleavage site (from reducing end (Glt20: DP2 product) or non-reducing end (Glt1, Glt3: DP4 products)), branching (Glt20) and linkage formed (1,3-linkage in Glt1, Glt3 and 1,6-linkage in Glt20). Hybrid models were built and stability of the resulting TIM-barrel structures was supported by molecular dynamics simulations. Catalytic amino acids were identified by superimposition of GH17 structures, and function was verified by mutagenesis using Glt20 as template (i.e., E120 and E209). Ligand docking revealed six putative subsites (−4, −3, −2, −1, +1 and +2), and the conserved interacting residues suggest substrate binding in the same orientation in all three transglycosylases, despite release of the donor oligosaccharide product from either the reducing (Glt20) or non-reducing end (Glt1, Gl3). Subsites +1 and +2 are most conserved and the difference in release is likely due to changes in loop structures, leading to loss of hydrogen bonds in Glt20. Substrate docking in Glt20 indicate that presence of covalently bound donor in glycone subsites −4 to −1 creates space to accommodate acceptor oligosaccharide in alternative subsites in the catalytic cleft, promoting a branching point and formation of a 1,6-linkage. The minimum donor size of DP5, can be explained assuming preferred binding of DP4 substrates in subsite −4 to −1, preventing catalysis.
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Biuppslag (personer, institutioner, konferenser, titlar ...)
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Jonsdottir, Lilja BjörkMatís ltd. – Icelandic food and biotech R&D
(författare)
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Hreggvidsson, Gudmundur O.University of Iceland,Matís ltd. – Icelandic food and biotech R&D
(författare)
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Fridjonsson, Olafur H.Matís ltd. – Icelandic food and biotech R&D
(författare)
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Watzlawick, HildegardUniversity of Stuttgart
(författare)
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Nordberg Karlsson, EvaLund University,Lunds universitet,Bioteknik,Centrum för tillämpade biovetenskaper,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biotechnology,Center for Applied Life Sciences,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH(Swepub:lu)biot-eno
(författare)
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BioteknikCentrum för tillämpade biovetenskaper
(creator_code:org_t)
Sammanhörande titlar
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Ingår i:Applied Sciences (Switzerland): MDPI AG11:92076-3417
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