Crystal Structure of the "cab"-type β Class Carbonic Anhydrase from the Archaeon Methanobacterium thermoautotrophicum

Pavel Strop, Kerry S. Smith, Tina M. Iverson, James Gregory Ferry, Douglas C. Rees

Research output: Contribution to journalArticle

107 Scopus citations

Abstract

The structure of the "cab"-type β class carbonic anhydrase from the archaeon Methanobacterium thermoautotrophicum (Cab) has been determined to 2.1-Å resolution using the multiwavelength anomalous diffraction phasing technique. Cab exists as a dimer with a subunit fold similar to that observed in "plant"-type β class carbonic anhydrases. The active site zinc is coordinated by protein ligands Cys 32, His87, and Cys90, with the tetrahedral coordination completed by a water molecule. The major difference between plant- and cab-type β class carbonic anhydrases is in the organization of the hydrophobic pocket. The structure reveals a Hepes buffer molecule bound 8 Å away from the active site zinc, which suggests a possible proton transfer pathway from the active site to the solvent.

Original languageEnglish (US)
Pages (from-to)10299-10305
Number of pages7
JournalJournal of Biological Chemistry
Volume276
Issue number13
DOIs
StatePublished - Mar 30 2001

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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