4HPP
Crystal structure of novel glutamine synthase homolog
Summary for 4HPP
| Entry DOI | 10.2210/pdb4hpp/pdb |
| Descriptor | Probable glutamine synthetase, MAGNESIUM ION, CALCIUM ION, ... (5 entities in total) |
| Functional Keywords | glutamine synthase homolog, glutamate, polyamine, ligase |
| Biological source | Pseudomonas aeruginosa |
| Total number of polymer chains | 1 |
| Total formula weight | 48165.97 |
| Authors | Ladner, J.E.,Atanasova, V.,Dolezelova, Z.,Parsons, J.F. (deposition date: 2012-10-24, release date: 2012-12-26, Last modification date: 2023-09-20) |
| Primary citation | Ladner, J.E.,Atanasova, V.,Dolezelova, Z.,Parsons, J.F. Structure and Activity of PA5508, a Hexameric Glutamine Synthetase Homologue. Biochemistry, 51:10121-10123, 2012 Cited by PubMed Abstract: The structure of PA5508 from Pseudomonas aeruginosa, a glutamine synthetase (GS) homologue, has been determined at 2.5 Å. Surprisingly, PA5508 forms single hexameric rings rather than the stacked double rings that are characteristic of GS. The C-terminal helical thong motif that links GS rings is present in PA5508; however, it is folded back toward the core of its own polypeptide, preventing it from interacting with a second ring. Interestingly, PA5508 displays a clear preference for aromatic amine substrates. Unique aspects of the structure illustrate how the enzyme is able to catalyze reactions involving bulky amines rather than ammonia. PubMed: 23234431DOI: 10.1021/bi3014856 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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