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Structure of a dimeric fungal α-type carbonic anhydrase

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  • Jose Antonio Cuesta-Seijo
  • Martin Simon Borchert
  • Jens-Christian Navarro-Poulsen
  • Kirk Matthew Schnorr
  • Steen Bennike Mortensen
  • Leila Lo Leggio
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The crystal structure of Aspergillus oryzae carbonic anhydrase (AoCA) was determined at 2.7Å resolution and it revealed a dimer, which only has precedents in the α class in two membrane and cancer-associated enzymes. α carbonic anhydrases are underrepresented in fungi compared to the β class, this being the first structural representative. The overall fold and zinc binding site resemble other well studied carbonic anhydrases. A major difference is that the histidine, thought to be the major proton shuttle residue in most mammalian enzymes, is replaced by a phenylalanine in AoCA. This finding poses intriguing questions as to the biological functions of fungal α carbonic anhydrases, which are promising candidates for biotechnological applications.
Original languageEnglish
JournalF E B S Letters
Volume585
Issue number7
Pages (from-to)1042-8
Number of pages7
ISSN0014-5793
DOIs
Publication statusPublished - 2011
Externally publishedYes

    Research areas

  • Amino Acid Sequence, Aspergillus oryzae, Carbonic Anhydrases, Crystallography, X-Ray, Humans, Models, Molecular, Molecular Sequence Data, Protein Multimerization, Protein Structure, Quaternary

ID: 33236717