2Q83

Crystal structure of ytaA (2635576) from Bacillus subtilis at 2.50 A resolution

2Q83 の概要

• エントリーDOI: 10.2210/pdb2q83/pdb
• 分子名称: YtaA protein, ADENOSINE, UNKNOWN LIGAND, ... (7 entities in total)
• 機能のキーワード: 2635576, ytaa, structural genomics, joint center for structural genomics, jcsg, protein structure initiative, psi-2, transferase
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 82222.68

構造登録者

Joint Center for Structural Genomics (JCSG) (登録日: 2007-06-08, 公開日: 2007-06-26, 最終更新日: 2024-10-16)

主引用文献

Scheeff, E.D.,Axelrod, H.L.,Miller, M.D.,Chiu, H.J.,Deacon, A.M.,Wilson, I.A.,Manning, G.
Genomics, evolution, and crystal structure of a new family of bacterial spore kinases.
Proteins, 78:1470-1482, 2010

PubMed Abstract: Bacterial spore formation is a complex process of fundamental relevance to biology and human disease. The spore coat structure is complex and poorly understood, and the roles of many of the protein components remain unclear. We describe a new family of spore coat proteins, the bacterial spore kinases (BSKs), and the first crystal structure of a BSK, YtaA (CotI) from Bacillus subtilis. BSKs are widely distributed in spore-forming Bacillus and Clostridium species, and have a dynamic evolutionary history. Sequence and structure analyses indicate that the BSKs are CAKs, a prevalent group of small molecule kinases in bacteria that is distantly related to the eukaryotic protein kinases. YtaA has substantial structural similarity to CAKs, but also displays distinctive features that broaden our understanding of the CAK group. Evolutionary constraint analysis of the protein surfaces indicates that members of the BSK family have distinct clade-conserved patterns in the substrate binding region, and probably bind and phosphorylate distinct targets. Several classes of BSKs have apparently independently lost catalytic activity to become pseudokinases, indicating that the family also has a major noncatalytic function.

PubMed: 20077512
DOI: 10.1002/prot.22663

実験手法

X-RAY DIFFRACTION (2.5 Å)