2ZZI

Crystal structure of TTHA1623 in a di-iron-bound form

2ZZI の概要

• エントリーDOI: 10.2210/pdb2zzi/pdb
• 関連するPDBエントリー: 2ZWR
• 分子名称: Metallo-beta-lactamase superfamily protein, FE (III) ION, ACETATE ION, ... (4 entities in total)
• 機能のキーワード: metallo-beta-lactamase, hydrolase
• 由来する生物種: Thermus thermophilus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 44984.76

構造登録者

Yamamura, A.,Okada, A.,Kameda, Y.,Ohtsuka, J.,Nakagawa, N.,Ebihara, A.,Yokoyama, S.,Kuramitsu, S.,Nagata, K.,Tanokura, M. (登録日: 2009-02-16, 公開日: 2010-01-05, 最終更新日: 2023-11-01)

主引用文献

Yamamura, A.,Okada, A.,Kameda, Y.,Ohtsuka, J.,Nakagawa, N.,Ebihara, A.,Nagata, K.,Tanokura, M.
Structure of TTHA1623, a novel metallo-beta-lactamase superfamily protein from Thermus thermophilus HB8
Acta Crystallogr.,Sect.F, 65:455-459, 2009

PubMed Abstract: TTHA1623 is a metallo-beta-lactamase superfamily protein from the extremely thermophilic bacterium Thermus thermophilus HB8. Homologues of TTHA1623 exist in a wide range of bacteria and archaea and one eukaryote, Giardia lamblia, but their function remains unknown. To analyze the structural properties of TTHA1623, the crystal structures of its iron-bound and zinc-bound forms have been determined to 2.8 and 2.2 A resolution, respectively. TTHA1623 possesses an alphabetabetaalpha-fold similar to that of other metallo-beta-lactamase superfamily proteins with glyoxalase II-type metal coordination. However, TTHA1623 exhibits a putative substrate-binding pocket with a unique shape.

PubMed: 19407375
DOI: 10.1107/S174430910901361X

実験手法

X-RAY DIFFRACTION (2.8 Å)