| 001 | 315680 | ||
| 005 | 20250730111431.0 | ||
| 024 | 7 | _ | |a 10.1074/jbc.M115.708495 |2 doi |
| 024 | 7 | _ | |a 0021-9258 |2 ISSN |
| 024 | 7 | _ | |a 1083-351X |2 ISSN |
| 024 | 7 | _ | |a WOS:000373299700023 |2 WOS |
| 024 | 7 | _ | |a 10.3204/PUBDB-2016-06026 |2 datacite_doi |
| 024 | 7 | _ | |a pmid:26823463 |2 pmid |
| 024 | 7 | _ | |a altmetric:5065209 |2 altmetric |
| 024 | 7 | _ | |a openalex:W2284437534 |2 openalex |
| 037 | _ | _ | |a PUBDB-2016-06026 |
| 041 | _ | _ | |a English |
| 082 | _ | _ | |a 570 |
| 100 | 1 | _ | |a Ramírez-Escudero, Mercedes |0 P:(DE-HGF)0 |b 0 |
| 245 | _ | _ | |a Structural Analysis of β-Fructofuranosidase from Xanthophyllomyces dendrorhous Reveals Unique Features and the Crucial Role of N-Glycosylation in Oligomerization and Activity |
| 260 | _ | _ | |a Bethesda, Md. |c 2016 |b Soc. |
| 336 | 7 | _ | |a article |2 DRIVER |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1486738419_28745 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 500 | _ | _ | |a (c) The American Society for Biochemistry and Molecular Biology, Inc.. This is a BioStructX funded project. |
| 520 | _ | _ | |a Xanthophyllomyces dendrorhous β-fructofuranosidase (XdINV)is a highly glycosylated dimeric enzyme that hydrolyzes sucrose and releases fructose from various fructooligosaccharides (FOS) and fructans. It also catalyzes the synthesis of FOS, prebiotics that stimulate the growth of beneficial bacteria in human gut. In contrast to most fructosylating enzymes, XdINV produces neo-FOS, which makes it an interesting biotechnology target. We present here its three-dimensional structure, which shows the expected bimodular arrangement and also a long extension of its C terminus that together with an N-linked glycan mediate the formation of an unusual dimer. The two active sites of the dimer are connected by a long crevice, which might indicate its potential ability to accommodate branched fructans. This arrangement could be representative of a group of GH32 yeast enzymes having the traits observed in XdINV. The inactive D80A mutant was used to obtain complexes with relevant substrates and products, with their crystals structures showing at least four binding subsites at each active site. Moreover, two different positions are observed from subsite +2 depending on the substrate, and thus, a flexible loop (Glu-334–His-343) is essential in binding sucrose and β(2–1)-linked oligosaccharides. Conversely, β(2–6) and neo-type substrates are accommodated mainly by stacking to Trp-105, explaining the production of neokestose and the efficient fructosylating activity of XdINV on α-glucosides. The role of relevant residues has been investigated by mutagenesis and kinetics measurements, and a model for the transfructosylating reaction has been proposed. The plasticity of its active site makes XdINV a valuable and flexible biocatalyst to produce novel bioconjugates. |
| 536 | _ | _ | |a 6G3 - PETRA III (POF3-622) |0 G:(DE-HGF)POF3-6G3 |c POF3-622 |f POF III |x 0 |
| 588 | _ | _ | |a Dataset connected to CrossRef |
| 693 | _ | _ | |a PETRA III |f PETRA Beamline P13 |1 EXP:(DE-H253)PETRAIII-20150101 |0 EXP:(DE-H253)P-P13-20150101 |6 EXP:(DE-H253)P-P13-20150101 |x 0 |
| 700 | 1 | _ | |a Gimeno-Pérez, María |0 P:(DE-HGF)0 |b 1 |
| 700 | 1 | _ | |a González, Beatriz |0 P:(DE-HGF)0 |b 2 |
| 700 | 1 | _ | |a Linde, Dolores |0 P:(DE-HGF)0 |b 3 |
| 700 | 1 | _ | |a Merdzo, Zoran |0 P:(DE-HGF)0 |b 4 |
| 700 | 1 | _ | |a Fernández-Lobato, María |0 P:(DE-HGF)0 |b 5 |e Corresponding author |
| 700 | 1 | _ | |a Sanz-Aparicio, Julia |0 P:(DE-HGF)0 |b 6 |e Corresponding author |
| 773 | _ | _ | |a 10.1074/jbc.M115.708495 |g Vol. 291, no. 13, p. 6843 - 6857 |0 PERI:(DE-600)1474604-9 |n 13 |p 6843 - 6857 |t The journal of biological chemistry |v 291 |y 2016 |x 1083-351X |
| 856 | 4 | _ | |u http://www.jbc.org/content/291/13/6843 |
| 856 | 4 | _ | |u https://bib-pubdb1.desy.de/record/315680/files/Structural_analysis_of_b-fructofuranosidase_from_X.pdf |y Published on 2016-01-28. Available in OpenAccess from 2017-01-28. |
| 856 | 4 | _ | |u https://bib-pubdb1.desy.de/record/315680/files/Structural_analysis_of_b-fructofuranosidase_from_X.gif?subformat=icon |x icon |y Published on 2016-01-28. Available in OpenAccess from 2017-01-28. |
| 856 | 4 | _ | |u https://bib-pubdb1.desy.de/record/315680/files/Structural_analysis_of_b-fructofuranosidase_from_X.jpg?subformat=icon-1440 |x icon-1440 |y Published on 2016-01-28. Available in OpenAccess from 2017-01-28. |
| 856 | 4 | _ | |u https://bib-pubdb1.desy.de/record/315680/files/Structural_analysis_of_b-fructofuranosidase_from_X.jpg?subformat=icon-180 |x icon-180 |y Published on 2016-01-28. Available in OpenAccess from 2017-01-28. |
| 856 | 4 | _ | |u https://bib-pubdb1.desy.de/record/315680/files/Structural_analysis_of_b-fructofuranosidase_from_X.jpg?subformat=icon-640 |x icon-640 |y Published on 2016-01-28. Available in OpenAccess from 2017-01-28. |
| 909 | C | O | |o oai:bib-pubdb1.desy.de:315680 |p openaire |p open_access |p VDB |p driver |p dnbdelivery |
| 913 | 1 | _ | |a DE-HGF |b Forschungsbereich Materie |l Von Materie zu Materialien und Leben |1 G:(DE-HGF)POF3-620 |0 G:(DE-HGF)POF3-622 |2 G:(DE-HGF)POF3-600 |v Facility topic: Research on Matter with Brilliant Light Sources |9 G:(DE-HGF)POF3-6G3 |x 0 |4 G:(DE-HGF)POF |3 G:(DE-HGF)POF3 |
| 914 | 1 | _ | |y 2016 |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0200 |2 StatID |b SCOPUS |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)1030 |2 StatID |b Current Contents - Life Sciences |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0600 |2 StatID |b Ebsco Academic Search |
| 915 | _ | _ | |a Embargoed OpenAccess |0 StatID:(DE-HGF)0530 |2 StatID |
| 915 | _ | _ | |a JCR |0 StatID:(DE-HGF)0100 |2 StatID |b J BIOL CHEM : 2015 |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0150 |2 StatID |b Web of Science Core Collection |
| 915 | _ | _ | |a WoS |0 StatID:(DE-HGF)0110 |2 StatID |b Science Citation Index |
| 915 | _ | _ | |a WoS |0 StatID:(DE-HGF)0111 |2 StatID |b Science Citation Index Expanded |
| 915 | _ | _ | |a IF < 5 |0 StatID:(DE-HGF)9900 |2 StatID |
| 915 | _ | _ | |a Peer Review |0 StatID:(DE-HGF)0030 |2 StatID |b ASC |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0310 |2 StatID |b NCBI Molecular Biology Database |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)1050 |2 StatID |b BIOSIS Previews |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0300 |2 StatID |b Medline |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0199 |2 StatID |b Thomson Reuters Master Journal List |
| 920 | 1 | _ | |0 I:(DE-H253)EMBL-User-20120814 |k EMBL-User |l EMBL-User |x 0 |
| 980 | _ | _ | |a journal |
| 980 | _ | _ | |a VDB |
| 980 | _ | _ | |a UNRESTRICTED |
| 980 | _ | _ | |a I:(DE-H253)EMBL-User-20120814 |
| 980 | 1 | _ | |a FullTexts |
| Library | Collection | CLSMajor | CLSMinor | Language | Author |
|---|
guest ::