Backbone 1H, 15N, and 13C resonance assignments of the Helicobacter pylori acyl carrier protein.
One of the small proteins from Helicobacter pylori, acyl carrier protein (ACP), was investigated by NMR. ACP is related to various cellular processes, especially with the biosynthesis of fatty acid. The basic NMR resonance assignment is a prerequisite for the validation of a heterologous protein interaction with ACP in H. pylori. Here, the results of the backbone (1)H, (15)N, and (13)C resonance assignments of the H. pylori ACP are reported using double- and triple-resonance techniques. About 97% of all of the (1)HN, (15)N, (13)CO, (13)Calpha, and (13)Cbeta resonances that cover 76 of the 78 non-proline residues are clarified through sequential- and specific- assignments. In addition, four helical regions were clearly identified on the basis of the resonance assignments.
Park
Sung Jean
SJ
Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul 151-742, Korea. lbj@nmr.snu.ac.kr
Kim
Ji-Sun
JS
Son
Woo-Sung
WS
Ahn
Hee Chul
HC
Lee
Bong Jin
BJ
D000213:Acyl Carrier Protein / Q000737:chemistry*; D002244:Carbon / Q000737:chemistry; D016480:Helicobacter pylori / Q000737:chemistry*; D006859:Hydrogen / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D009584:Nitrogen / Q000737:chemistry
D000213:Acyl Carrier Protein; D002244:Carbon; D006859:Hydrogen; D009584:Nitrogen