Analysis of the binding site of NagS and activity of NagS mutants.

<p><b>(a)</b> NagS active site with bound GlcNAc-6P (gray carbons), protein residues are coloured with pale blue and yellow carbons to indicate the 2 monomers forming the active site. 2|Fo|-|Fc| electron density contoured at 1.2 σ is shown as cyan mesh. Hydrogen bonds are indicated...

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Detaylı Bibliyografya
Yazar:	Chao Li (145513) (author)
Diğer Yazarlar:	Mia Urem (22683580) (author), Ioli Kotsogianni (9930187) (author), Josephine Lau (20442343) (author), Chao Du (288036) (author), Somayah S. Elsayed (9192571) (author), Nathaniel I. Martin (847378) (author), Iain W. McNae (840777) (author), Patrick Voskamp (2311429) (author), Christoph Mayer (57204) (author), Sébastien Rigali (724082) (author), Navraj Pannu (10163763) (author), Jan Pieter Abrahams (1429531) (author), Lennart Schada von Borzyskowski (22683583) (author), Gilles P. van Wezel (7838948) (author)
Baskı/Yayın Bilgisi:	2025
Konular:	Biochemistry Microbiology Ecology Developmental Biology Inorganic Chemistry Biological Sciences not elsewhere classified controls nutrient signaling also revealed 6 highlighted key residues glcnac sensing requires toxicity pathway dependent 6p deacetylase naga novel glcnac 6 key role substrate glcnac novel enzyme work uncovers wall leads unprecedented reaction substrate mycelium structural analogue streptomycetaceae </ streptomyces </ revolves around promiscuous activity nature ’ n </ multicellular lifestyle metabolic checkpoint medicine makers lytic dismantling landmark event hyphal cell highly conserved growth media function analysis clinical antibiotics central metabolism catalytic inhibitor antibiotic production active site >- acetylglucosamine 6p dehydratase
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Analysis of the binding site of NagS and activity of NagS mutants.

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