7UWQ

Klebsiella pneumoniae adenosine monophosphate nucleosidase

7UWQ の概要

• エントリーDOI: 10.2210/pdb7uwq/pdb
• EMDBエントリー: 26838
• 分子名称: AMP nucleosidase (1 entity in total)
• 機能のキーワード: nucleosidase, amp, salvage, hydrolase
• 由来する生物種: Klebsiella pneumoniae
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 331958.02

構造登録者

Richardson, B.C.,French, J.B. (登録日: 2022-05-03, 公開日: 2022-09-28, 最終更新日: 2024-06-12)

主引用文献

Richardson, B.C.,Shek, R.,Van Voorhis, W.C.,French, J.B.
Structure of Klebsiella pneumoniae adenosine monophosphate nucleosidase.
Plos One, 17:e0275023-e0275023, 2022

PubMed Abstract: Klebsiella pneumoniae is a bacterial pathogen that is increasingly responsible for hospital-acquired pneumonia and sepsis. Progressive development of antibiotic resistance has led to higher mortality rates and creates a need for novel treatments. Because of the essential role that nucleotides play in many bacterial processes, enzymes involved in purine and pyrimidine metabolism and transport are ideal targets for the development of novel antibiotics. Herein we describe the structure of K. pneumoniae adenosine monophosphate nucleosidase (KpAmn), a purine salvage enzyme unique to bacteria, as determined by cryoelectron microscopy. The data detail a well conserved fold with a hexameric overall structure and clear density for the putative active site residues. Comparison to the crystal structures of homologous prokaryotic proteins confirms the presence of many of the conserved structural features of this protein yet reveals differences in distal loops in the absence of crystal contacts. This first cryo-EM structure of an Amn enzyme provides a basis for future structure-guided drug development and extends the accuracy of structural characterization of this family of proteins beyond this clinically relevant organism.

PubMed: 36264993
DOI: 10.1371/journal.pone.0275023

実験手法

ELECTRON MICROSCOPY (3.05 Å)