4GQX

Crystal structure of EIIA(NTR) from Burkholderia pseudomallei

4GQX の概要

• エントリーDOI: 10.2210/pdb4gqx/pdb
• 分子名称: PTS IIA-like nitrogen-regulatory protein PtsN (1 entity in total)
• 機能のキーワード: eiia(ntr), alpha/beta, histidine containing phosphocarrier protein, npr, ei(ntr), na, transferase
• 由来する生物種: Burkholderia pseudomallei
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 36297.43

構造登録者

Kim, M.-S.,Shin, D.H. (登録日: 2012-08-24, 公開日: 2013-03-20, 最終更新日: 2024-03-20)

主引用文献

Kim, M.-S.,Lee, H.,Heo, L.,Lim, A.,Seok, C.,Shin, D.H.
New molecular interaction of IIA(Ntr) and HPr from Burkholderia pseudomallei identified by X-ray crystallography and docking studies
Proteins, 81:1499-1508, 2013

PubMed Abstract: The nitrogen-related phosphoenolpyruvate phosphotransferase system (PTS(Ntr) ) is involved in controlling ammonia assimilation and nitrogen fixation. The additional role of PTS(Ntr) as a regulatory link between nitrogen and carbon utilization in Escherichia coli is assumed to be closely related to molecular functions of IIA(Ntr) in potassium homeostasis. We have determined the crystal structure of IIA(Ntr) from Burkholderia pseudomallei (BpIIA(Ntr) ), which is a causative agent of melioidosis. The crystal structure of dimeric BpIIA(Ntr) determined at 3.0 Å revealed that its active sites are mutually blocked. This dimeric state is stabilized by charge and weak hydrophobic interactions. Overall monomeric structure and the active site residues, Arg51 and His67, of BpIIA(Ntr) are well conserved with those of IIA(Ntr) enzymes from E. coli and Neisseria meningitides. Interestingly, His113 of BpIIA(Ntr) , which corresponds to a key residue in another phosphoryl group relay in the mannitol-specific enzyme EIIA family (EIIA(Mtl) ), is located away from the active site due to the loop connecting β5 and α3. Combined with other differences in molecular surface properties, these structural signatures distinguish the IIA(Ntr) family from the EIIA(Mtl) family. Since, there is no gene for NPr in the chromosome of B. pseudomallei, modeling and docking studies of the BpIIA(Ntr) -BpHPr complex has been performed to support the proposal on the NPr-like activity of BpHPr. A potential dual role of BpHPr as a nonspecific phosphocarrier protein interacting with both sugar EIIAs and IIA(Ntr) in B. pseudomallei has been discussed.

PubMed: 23483653
DOI: 10.1002/prot.24275

実験手法

X-RAY DIFFRACTION (3 Å)