Dijkstra, BW

Duine, JA

Kalk, KH

Oubrie, A

Rozeboom, HJ

English

The crystal structure of a dimeric apo form of the soluble quinoprotein glucose dehydrogenase (s-GDH) from Acinetobacter calcoaceticus has been solved by multiple isomorphous replacement followed by density modification, and was subsequently refined at 1.72 Angstrom resolution to a final crystallographic R-factor of 16.5 % and free R-factor of 0.8 %. The s-GDH monomer has a beta-propeller fold consisting of six four-stranded anti-parallel beta-sheets aligned around a pseudo 6-fold symmetry axis. The enzyme binds three calcium ions per monomer, two of which are located in the dimer interface. The third is bound in the putative active site, where it may bind and functionalize the pyrroloquinoline quinone (PQQ) cofactor. A data base search unexpectedly showed that four uncharacterized protein sequences are homologous to s-GDH with many residues in the putative active site absolutely conserved. This indicates that these homologs may have a similar structure and that they may catalyze similar PQQ-dependent reactions.A structure-based sequence alignment of the six four-stranded beta-sheets in s-GDH's beta-propeller fold shows an internally conserved sequence repeat that gives rise to two distinct conserved structural motifs. The first structural motif is found at the corner of the short beta-turn between the inner two beta-strands of the beta-sheets, where an Asp side-chain points back into the beta-sheet to form a hydrogen-bond with the OH/NH of a Tyr/Trp side-chain in the same beta-sheet. The second motif involves an Arg/Lys side-chain in the C beta-strand of one beta-sheet, which forms a bidentate salt-bridge with an Asp/Glu in the CD loop of the next beta-sheet. These intra and inter-beta-sheet hydrogen-bonds are likely to contribute to the stability of the s-GDH beta-propeller fold. (C) 1999 Academic Press.</p

Dissertations of the University of Groningen

   University of GroningenThe 1.7 angstrom crystal structure of the apo form of the soluble quinoprotein glucosedehydrogenase from Acinetobacter calcoaceticus reveals a novel internal conservedsequence repeatOubrie, A; Rozeboom, HJ; Kalk, KH; Duine, JA; Dijkstra, BWPublished in:Journal of Molecular BiologyIMPORTANT NOTE: You are advised to consult the publisher's version (publisher's PDF) if you wish to cite fromit. Please check the document version below.Document VersionPublisher's PDF, also known as Version of recordPublication date:1999Link to publication in University of Groningen/UMCG research databaseCitation for published version (APA):Oubrie, A., Rozeboom, HJ., Kalk, KH., Duine, JA., & Dijkstra, BW. (1999). The 1.7 angstrom crystalstructure of the apo form of the soluble quinoprotein glucose dehydrogenase from Acinetobactercalcoaceticus reveals a novel internal conserved sequence repeat. Journal of Molecular Biology, 289(2),319-333.CopyrightOther than for strictly personal use, it is not permitted to download or to forward/distribute the text or part of it without the consent of theauthor(s) and/or copyright holder(s), unless the work is under an open content license (like Creative Commons).The publication may also be distributed here under the terms of Article 25fa of the Dutch Copyright Act, indicated by the “Taverne” license.More information can be found on the University of Groningen website: https://www.rug.nl/library/open-access/self-archiving-pure/taverne-amendment.Take-down policyIf you believe that this document breaches copyright please contact us providing details, and we will remove access to the work immediatelyand investigate your claim.Article No. 3092 available online at http://www.idealibrary.com on J. Mol. Biol. (1999) 292, 19100ERRATUMThe 1.7 AÊ Crystal Structure of the Apo Form of theSoluble Quinoprotein Glucose Dehydrogenase fromAcinetobacter calcoaceticus Reveals a Novel InternalConserved Sequence RepeatArthur Oubrie, HenrieÈ tte J. Rozeboom, Kor H. KalkJohannis A. Duine and Bauke W. DijkstraJ. Mol. Biol. (1999) 289, 319±333It is regretted that an error occurred in the above paper. In the Abstract and Results and Discussionsections the free R-factor value was listed as 0.8 % instead of 20.8 %. The corrected sentences are givenbelow.The ®rst sentence of the abstract should read:The crystal structure of a dimeric apo form of the soluble quinoprotein glucose dehydrogenase (s-GDH)from Acinetobacter calcoaceticus has been solved by multiple isomorphous replacement followed by densitymodi®cation, and was subsequently re®ned at 1.72 AÊ resolution to a ®nal crystallographic R-factor of16.5 % and free R-factor of 20.8 %.The ®rst senctence of the `Re®nement and quality of the model' section in the Results and Discussionshould read:Final crystallographic (Rcrys) and free (Rfree: BruÈ nger, 1992) R-factor values of 16.5 % and 20.8 %, respect-ively, were obtained for data from 20.0 to 1.72 AÊ resolution (no s cut-off).22-2836/99/360191±1 $30.00/0 # 1999 Academic Press

The 1.7 angstrom crystal structure of the apo form of the soluble quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus reveals a novel internal conserved sequence repeat

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The 1.7 angstrom crystal structure of the apo form of the soluble quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus reveals a novel internal conserved sequence repeat

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