7AX5
Anammox-specific acyl carrier protein from Kuenenia stuttgartiensis; ensemble refinement
Summary for 7AX5
| Entry DOI | 10.2210/pdb7ax5/pdb |
| Descriptor | Similar to acyl carrier protein, ZINC ION (3 entities in total) |
| Functional Keywords | anammox, ladderane, acyl carrier protein, ensemble refinement, lipid binding protein |
| Biological source | Kuenenia stuttgartiensis |
| Total number of polymer chains | 1 |
| Total formula weight | 11190.00 |
| Authors | Dietl, A.,Barends, T. (deposition date: 2020-11-09, release date: 2021-08-11, Last modification date: 2024-06-19) |
| Primary citation | Dietl, A.,Barends, T.R.M. Dynamics in an unusual acyl carrier protein from a ladderane lipid-synthesizing organism. Proteins, 90:73-82, 2022 Cited by PubMed Abstract: Anaerobic ammonium-oxidizing (anammox) bacteria express a distinct acyl carrier protein implicated in the biosynthesis of the highly unusual "ladderane" lipids these organisms produce. This "anammox-specific" ACP, or amxACP, shows several unique features such as a conserved FF motif and an unusual sequence in the functionally important helix III. Investigation of the protein's structure and dynamics, both in the crystal by ensemble refinement and by MD simulations, reveals that helix III adopts a rare six-residue-long 3 -helical conformation that confers a large degree of conformational and positional variability on this part of the protein. This way of introducing structural flexibility by using the inherent properties of 3 -helices appears unique among ACPs. Moreover, the structure suggests a role for the FF motif in shielding the thioester linkage between the protein's prosthetic group and its acyl cargo from hydrolysis. PubMed: 34310758DOI: 10.1002/prot.26187 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.756 Å) |
Structure validation
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