9IQ8
Ankyrin-like protein, AnkB
Summary for 9IQ8
Entry DOI | 10.2210/pdb9iq8/pdb |
Descriptor | Ankyrin-like protein AnkB (2 entities in total) |
Functional Keywords | ankb, ankyrin repeat domain-containing protein, signal transduction mechanisms, signaling protein |
Biological source | Acinetobacter baumannii |
Total number of polymer chains | 4 |
Total formula weight | 70352.44 |
Authors | |
Primary citation | Sung, J.H.,Lee, S.Y.,Lee, C.S.,Lee, J.H.,Park, H.H. Structural analysis of a bacterial ankyrin-like protein secreted by Acinetobacter baumannii. Biochem.Biophys.Res.Commun., 733:150573-150573, 2024 Cited by PubMed Abstract: In bacteria, the ankyrin-like protein AnkB helps overcome stress by regulating catalase activity when expressed under stressful conditions. As the structural properties of AnkB are largely unexplored, our understanding of various AnkB-mediated functions in bacteria remains limited. In the present study, we describe the structure of AnkB from Acinetobacter baumannii, hereafter referred to as "AbAnkB," which has a unique tertiary configuration compared with that of other ankyrin domain-containing proteins. Structural analysis revealed that AbAnkB has a relatively long loop between AKR3 and AKR4 and an oppositely positioned α helix. Based on amino acid conservation and protein surface analyses, we identified a hydrophobic patch that might be critical for the function of AbAnkB. To the best of our knowledge, our study is the first to report the structure of a bacterial AnkB protein; our findings will markedly enhance our understanding of its functions in bacteria. PubMed: 39208644DOI: 10.1016/j.bbrc.2024.150573 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.42 Å) |
Structure validation
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