5O7B

CRYSTAL STRUCTURE OF THE SLR0328 TYROSINE PHOSPHATASE WZB FROM SYNECHOCYSTIS SP. PCC 6803

5O7B の概要

• エントリーDOI: 10.2210/pdb5o7b/pdb
• 分子名称: Putative low molecular weight protein-tyrosine-phosphatase slr0328 (2 entities in total)
• 機能のキーワード: phosphatase, hydrolase
• 由来する生物種: Synechocystis sp. (strain PCC 6803 / Kazusa)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18939.31

構造登録者

Leite, J.P.,Gales, L. (登録日: 2017-06-08, 公開日: 2018-06-20, 最終更新日: 2024-01-17)

主引用文献

Pereira, S.B.,Santos, M.,Leite, J.P.,Flores, C.,Eisfeld, C.,Buttel, Z.,Mota, R.,Rossi, F.,De Philippis, R.,Gales, L.,Morais-Cabral, J.H.,Tamagnini, P.
The role of the tyrosine kinase Wzc (Sll0923) and the phosphatase Wzb (Slr0328) in the production of extracellular polymeric substances (EPS) by Synechocystis PCC 6803.
Microbiologyopen, :e753-e753, 2019

PubMed Abstract: Many cyanobacteria produce extracellular polymeric substances (EPS) mainly composed of heteropolysaccharides with unique characteristics that make them suitable for biotechnological applications. However, manipulation/optimization of EPS biosynthesis/characteristics is hindered by a poor understanding of the production pathways and the differences between bacterial species. In this work, genes putatively related to different pathways of cyanobacterial EPS polymerization, assembly, and export were targeted for deletion or truncation in the unicellular Synechocystis sp. PCC 6803. No evident phenotypic changes were observed for some mutants in genes occurring in multiple copies in Synechocystis genome, namely ∆wzy (∆sll0737), ∆wzx (∆sll5049), ∆kpsM (∆slr2107), and ∆kpsM∆wzy (∆slr2107∆sll0737), strongly suggesting functional redundancy. In contrast, Δwzc (Δsll0923) and Δwzb (Δslr0328) influenced both the amount and composition of the EPS, establishing that Wzc participates in the production of capsular (CPS) and released (RPS) polysaccharides, and Wzb affects RPS production. The structure of Wzb was solved (2.28 Å), revealing structural differences relative to other phosphatases involved in EPS production and suggesting a different substrate recognition mechanism. In addition, Wzc showed the ATPase and autokinase activities typical of bacterial tyrosine kinases. Most importantly, Wzb was able to dephosphorylate Wzc in vitro, suggesting that tyrosine phosphorylation/dephosphorylation plays a role in cyanobacterial EPS production.

PubMed: 30675753
DOI: 10.1002/mbo3.753

実験手法

X-RAY DIFFRACTION (2.281 Å)