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  • Valegård, KarinSwedish University of Agricultural Sciences,Sveriges lantbruksuniversitet,Uppsala universitet,Institutionen för cell- och molekylärbiologi,Molecular Biophysics,Institutionen för molekylärbiologi,Department of Molecular Biology (author)

Structural and mechanistic studies of the orf12 gene product from the clavulanic acid biosynthesis pathway

  • Article/chapterEnglish2013

Publisher, publication year, extent ...

  • 2013
  • printrdacarrier

Numbers

  • LIBRIS-ID:oai:DiVA.org:uu-206559
  • https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-206559URI
  • https://doi.org/10.1107/S0907444913011013DOI
  • https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-291534URI
  • https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-287543URI
  • https://res.slu.se/id/publ/54503URI

Supplementary language notes

  • Language:English
  • Summary in:English

Part of subdatabase

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  • Subject category:ref swepub-contenttype
  • Subject category:art swepub-publicationtype

Notes

  • Structural and biochemical studies of the orf12 gene product (ORF12) from the clavulanic acid (CA) biosynthesis gene cluster are described. Sequence and crystallographic analyses reveal two domains: a C-terminal penicillin-binding protein (PBP)/beta-lactamase-type fold with highest structural similarity to the class A beta-lactamases fused to an N-terminal domain with a fold similar to steroid isomerases and polyketide cyclases. The C-terminal domain of ORF12 did not show beta-lactamase or PBP activity for the substrates tested, but did show low-level esterase activity towards 3'-O-acetyl cephalosporins and a thioester substrate. Mutagenesis studies imply that Ser173, which is present in a conserved SXXK motif, acts as a nucleophile in catalysis, consistent with studies of related esterases, beta-lactamases and d-Ala carboxypeptidases. Structures of wild-type ORF12 and of catalytic residue variants were obtained in complex with and in the absence of clavulanic acid. The role of ORF12 in clavulanic acid biosynthesis is unknown, but it may be involved in the epimerization of (3S,5S)-clavaminic acid to (3R,5R)-clavulanic acid.

Subject headings and genre

Added entries (persons, corporate bodies, meetings, titles ...)

  • Iqbal, Aman (author)
  • Kershaw, Nadia J. (author)
  • Ivison, David (author)
  • Genereux, Catherine (author)
  • Dubus, Alain (author)
  • Blikstad, CeciliaUppsala universitet,Biokemi(Swepub:uu)cecbl752 (author)
  • Demetriades, Marina (author)
  • Hopkinson, Richard J. (author)
  • Lloyd, Adrian J. (author)
  • Roper, David I. (author)
  • Schofield, Christopher J. (author)
  • Andersson, IngerDepartment of Molecular Biology, Swedish University of Agricultural Sciences(Swepub:uu)inand172 (author)
  • McDonough, Michael A. (author)
  • Uppsala universitetInstitutionen för cell- och molekylärbiologi (creator_code:org_t)
  • Sveriges lantbruksuniversitet

Related titles

  • In:Acta Crystallographica Section D69, s. 1567-15790907-44491399-0047

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