Evolutionary relationship between the bacterial HPr kinase and the ubiquitous PEP‐carboxykinase: expanding the P‐loop nucleotidyl transferase superfamily

FEBS Letters

Scheffzek, Klaus²  Russell, Robert B.²  Hengstenberg, Wolfgang¹  Márquez, José Antonio² 

[1] Department of Biology, Ruhr-Universität Bochum, Universitätstrasse 150, 44780 Bochum, Germany;Structural and Computational Biology Programme, EMBL, Meyerhofstrasse 1, D-69117 Heidelberg, Germany

关键词: Protein structure similarity;    Histidine phosphocarrier protein kinase;    Phosphoenolpyruvate carboxykinase;    P-loop;    Evolution;   

DOI  :  10.1016/S0014-5793(02)02518-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Similarities between protein three-dimensional structures can reveal evolutionary and functional relationships not apparent from sequence comparison alone. Here we report such a similarity between the metabolic enzymes histidine phosphocarrier protein kinase (HPrK) and phosphoenolpyruvate carboxykinase (PCK), suggesting that they are evolutionarily related. Current structure classifications place PCK and other P-loop containing nucleotidyl-transferases into different folds. Our comparison of both HPrK and PCK to other P-loop containing proteins reveals that all share a common structural motif consisting of an αβ segment containing the P-loop flanked by an additional β-strand that is adjacent in space, but far apart along the sequence. Analysis also shows that HPrK/PCK differ from other P-loop containing structures no more than they differ from each other. We thus suggest that HPrK and PCK should be classified with other P-loop containing proteins, and that all probably share a common ancestor that probably contained a simple P-loop motif with different protein segments being added or lost over the course of evolution. We used the structure-based sequence alignment containing residues specific to HPrK/PCK to identify additional members of this P-loop containing family.

【 授权许可】

Unknown