1G5C

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

1G5C の概要

• エントリーDOI: 10.2210/pdb1g5c/pdb
• 関連するPDBエントリー: 1ddz 1ekj
• 分子名称: BETA-CARBONIC ANHYDRASE, ZINC ION, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: beta carbonic anhydrase, zinc, hepes, lyase
• 由来する生物種: Methanothermobacter thermautotrophicus
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 114566.20

構造登録者

Strop, P.,Smith, K.S.,Iverson, T.M.,Ferry, J.G.,Rees, D.C. (登録日: 2000-10-31, 公開日: 2001-04-04, 最終更新日: 2024-02-07)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.1 Å)