2VED

crystal structure of the chimerical mutant CapABK55M protein

2VED の概要

• エントリーDOI: 10.2210/pdb2ved/pdb
• 分子名称: MEMBRANE PROTEIN CAPA1, PROTEIN TYROSINE KINASE, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: co-polymerase, activation mechanism, chimera, transferase, bacterial tyrosine-kinase, exopolysaccharide synthesis
• 由来する生物種: STAPHYLOCOCCUS AUREUS
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 60904.52

構造登録者

Olivares-Illana, V.,Meyer, P.,Gueguen-Chaignon, V.,Soulat, D.,Deustcher, J.,Cozzone, A.J.,Morera, S.,Grangeasse, C.,Nessler, S. (登録日: 2007-10-19, 公開日: 2008-07-01, 最終更新日: 2023-12-13)

主引用文献

Olivares-Illana, V.,Meyer, P.,Bechet, E.,Gueguen-Chaignon, V.,Soulat, D.,Lazereg-Riquier, S.,Mijakovic, I.,Deutscher, J.,Cozzone, A.J.,Laprevote, O.,Morera, S.,Grangeasse, C.,Nessler, S.
Structural Basis for the Regulation Mechanism of the Tyrosine Kinase Capb from Staphylococcus Aureus.
Plos Biol., 6:E143-, 2008

PubMed Abstract: Bacteria were thought to be devoid of tyrosine-phosphorylating enzymes. However, several tyrosine kinases without similarity to their eukaryotic counterparts have recently been identified in bacteria. They are involved in many physiological processes, but their accurate functions remain poorly understood due to slow progress in their structural characterization. They have been best characterized as copolymerases involved in the synthesis and export of extracellular polysaccharides. These compounds play critical roles in the virulence of pathogenic bacteria, and bacterial tyrosine kinases can thus be considered as potential therapeutic targets. Here, we present the crystal structures of the phosphorylated and unphosphorylated states of the tyrosine kinase CapB from the human pathogen Staphylococcus aureus together with the activator domain of its cognate transmembrane modulator CapA. This first high-resolution structure of a bacterial tyrosine kinase reveals a 230-kDa ring-shaped octamer that dissociates upon intermolecular autophosphorylation. These observations provide a molecular basis for the regulation mechanism of the bacterial tyrosine kinases and give insights into their copolymerase function.

PubMed: 18547145
DOI: 10.1371/JOURNAL.PBIO.0060143

実験手法

X-RAY DIFFRACTION (2.6 Å)