1g5c
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CRYSTAL STRUCTURE OF THE 'CAB' TYPE BETA CLASS CARBONIC ANHYDRASE FROM METHANOBACTERIUM THERMOAUTOTROPHICUM
OverviewOverview
The structure of the "cab"-type beta class carbonic anhydrase from the, archaeon Methanobacterium thermoautotrophicum (Cab) has been determined to, 2.1-A resolution using the multiwavelength anomalous diffraction phasing, technique. Cab exists as a dimer with a subunit fold similar to that, observed in "plant"-type beta class carbonic anhydrases. The active site, zinc is coordinated by protein ligands Cys(32), His(87), and Cys(90), with, the tetrahedral coordination completed by a water molecule. The major, difference between plant- and cab-type beta class carbonic anhydrases is, in the organization of the hydrophobic pocket. The structure reveals a, Hepes buffer molecule bound 8 A away from the active site zinc, which, suggests a possible proton transfer pathway from the active site to the, solvent.
About this StructureAbout this Structure
1G5C is a Single protein structure of sequence from Methanothermobacter thermautotrophicus with ZN, CA and EPE as ligands. Active as Carbonate dehydratase, with EC number 4.2.1.1 Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the "cab"-type beta class carbonic anhydrase from the archaeon Methanobacterium thermoautotrophicum., Strop P, Smith KS, Iverson TM, Ferry JG, Rees DC, J Biol Chem. 2001 Mar 30;276(13):10299-305. Epub 2000 Nov 28. PMID:11096105
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