1G5C

CRYSTAL STRUCTURE OF THE 'CAB' TYPE BETA CLASS CARBONIC ANHYDRASE FROM METHANOBACTERIUM THERMOAUTOTROPHICUM

Summary for 1G5C

• Entry DOI: 10.2210/pdb1g5c/pdb
• Related: 1ddz 1ekj
• Descriptor: BETA-CARBONIC ANHYDRASE, ZINC ION, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: beta carbonic anhydrase, zinc, hepes, lyase
• Biological source: Methanothermobacter thermautotrophicus
• Total number of polymer chains: 6
• Total formula weight: 114566.20

Authors

Strop, P.,Smith, K.S.,Iverson, T.M.,Ferry, J.G.,Rees, D.C. (deposition date: 2000-10-31, release date: 2001-04-04, Last modification date: 2024-02-07)

Primary citation

Strop, P.,Smith, K.S.,Iverson, T.M.,Ferry, J.G.,Rees, D.C.
Crystal structure of the "cab"-type beta class carbonic anhydrase from the archaeon Methanobacterium thermoautotrophicum.
J.Biol.Chem., 276:10299-10305, 2001

PubMed Abstract: 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.

PubMed: 11096105
DOI: 10.1074/jbc.M009182200

Experimental method

X-RAY DIFFRACTION (2.1 Å)