3TIS

Crystal structures of yrdA from Escherichia coli, a homologous protein of gamma-class carbonic anhydrases, show possible allosteric conformations

3TIS の概要

• エントリーDOI: 10.2210/pdb3tis/pdb
• 関連するPDBエントリー: 3TIO
• 分子名称: Protein YrdA, ZINC ION (3 entities in total)
• 機能のキーワード: carbonic anhydrase (ca), zn biding, phosphate binding, transferase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 60546.49

構造登録者

Park, H.M.,Chio, J.W.,Lee, J.E.,Jung, J.H.,Kim, B.Y.,Kim, J.S. (登録日: 2011-08-21, 公開日: 2012-08-01, 最終更新日: 2024-03-20)

主引用文献

Park, H.M.,Park, J.H.,Choi, J.W.,Lee, J.E.,Kim, B.Y.,Jung, C.H.,Kim, J.S.
Structures of the gamma-class carbonic anhydrase homologue YrdA suggest a possible allosteric switch
Acta Crystallogr.,Sect.D, 68:920-926, 2012

PubMed Abstract: The YrdA protein shows high sequence similarity to γ-class carbonic anhydrase (γ-CA) proteins and is classified as part of the γ-CA protein family. However, its function has not been fully elucidated as it lacks several of the conserved residues that are considered to be necessary for γ-CA catalysis. Interestingly, a homologue of γ-CA from Methanosarcina thermophila and a β-carboxysomal γ-CA from a β-cyanobacterium have shown that these catalytic residues are not always conserved in γ-CAs. The crystal structure of YrdA from Escherichia coli (ecYrdA) is reported here in two crystallographic forms. The overall structure of ecYrdA is also similar to those of the γ-CAs. One loop around the putative catalytic site shows a number of alternative conformations. A His residue (His70) on this loop coordinates with, or is reoriented from, the catalytic Zn(2+) ion; this is similar to the conformations mediated by an Asp residue on the catalytic loops of β-CA proteins. One Trp residue (Trp171) also adopts two alternative conformations that may be related to the spatial positions of the catalytic loop. Even though significant CA activity could not be detected using purified ecYrdA, these structural features have potential functional implications for γ-CA-related proteins.

PubMed: 22868757
DOI: 10.1107/S0907444912017210

実験手法

X-RAY DIFFRACTION (2.3 Å)