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2FGY

Beta Carbonic Anhydrase from the Carboxysomal Shell of Halothiobacillus neapolitanus (CsoSCA)

2FGY の概要
エントリーDOI10.2210/pdb2fgy/pdb
分子名称carboxysome shell polypeptide, ZINC ION (3 entities in total)
機能のキーワードbeta class of carbonic anhydrase, lyase
由来する生物種Halothiobacillus neapolitanus
タンパク質・核酸の鎖数2
化学式量合計121697.93
構造登録者
Sawaya, M.R. (登録日: 2005-12-22, 公開日: 2006-01-17, 最終更新日: 2024-11-13)
主引用文献Sawaya, M.R.,Cannon, G.C.,Heinhorst, S.,Tanaka, S.,Williams, E.B.,Yeates, T.O.,Kerfeld, C.A.
The Structure of beta-carbonic anhydrase from the carboxysomal shell reveals a distinct subclass with one active site for the price of two.
J.Biol.Chem., 281:7546-7555, 2006
Cited by
PubMed Abstract: CsoSCA (formerly CsoS3) is a bacterial carbonic anhydrase localized in the shell of a cellular microcompartment called the carboxysome, where it converts HCO(3)(-) to CO(2) for use in carbon fixation by ribulose-bisphosphate carboxylase/oxygenase (RuBisCO). CsoSCA lacks significant sequence similarity to any of the four known classes of carbonic anhydrase (alpha, beta, gamma, or delta), and so it was initially classified as belonging to a new class, epsilon. The crystal structure of CsoSCA from Halothiobacillus neapolitanus reveals that it is actually a representative member of a new subclass of beta-carbonic anhydrases, distinguished by a lack of active site pairing. Whereas a typical beta-carbonic anhydrase maintains a pair of active sites organized within a two-fold symmetric homodimer or pair of fused, homologous domains, the two domains in CsoSCA have diverged to the point that only one domain in the pair retains a viable active site. We suggest that this defunct and somewhat diminished domain has evolved a new function, specific to its carboxysomal environment. Despite the level of sequence divergence that separates CsoSCA from the other two subclasses of beta-carbonic anhydrases, there is a remarkable level of structural similarity among active site regions, which suggests a common catalytic mechanism for the interconversion of HCO(3)(-) and CO(2). Crystal packing analysis suggests that CsoSCA exists within the carboxysome shell either as a homodimer or as extended filaments.
PubMed: 16407248
DOI: 10.1074/jbc.M510464200
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.2 Å)
構造検証レポート
Validation report summary of 2fgy
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-02-11に公開中

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