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PDBsum entry 4hpp
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References listed in PDB file
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Key reference
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Title
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Structure and activity of pa5508, A hexameric glutamine synthetase homologue.
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Authors
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J.E.Ladner,
V.Atanasova,
Z.Dolezelova,
J.F.Parsons.
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Ref.
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Biochemistry, 2012,
51,
10121-10123.
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PubMed id
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Abstract
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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.
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