Lysine-cysteine NOS bonds
From Proteopedia
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==Methods== | ==Methods== | ||
| - | [[6zx4]] (oxidized form, NOS present) has a [[resolution]] of 0.96 Å, with a better than average [[Rfree|R<sub>free</sub>]] of 0.136. | + | This is a summary of the observations supporting the NOS bond<ref name="wensien2021" />. [[6zx4]] (oxidized form, NOS present) has a [[resolution]] of 0.96 Å, with a better than average [[Rfree|R<sub>free</sub>]] of 0.136. ''Neisseria gonorrhoeae'' transaldolase has 3 cysteines (no disulfide bonds). It does not form disulfide-linked oligomers. |
==References== | ==References== | ||
<references /> | <references /> | ||
Revision as of 18:15, 26 May 2021
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Methods
This is a summary of the observations supporting the NOS bond[1]. 6zx4 (oxidized form, NOS present) has a resolution of 0.96 Å, with a better than average Rfree of 0.136. Neisseria gonorrhoeae transaldolase has 3 cysteines (no disulfide bonds). It does not form disulfide-linked oligomers.
References
- ↑ 1.0 1.1 1.2 1.3 1.4 1.5 Wensien M, von Pappenheim FR, Funk LM, Kloskowski P, Curth U, Diederichsen U, Uranga J, Ye J, Fang P, Pan KT, Urlaub H, Mata RA, Sautner V, Tittmann K. A lysine-cysteine redox switch with an NOS bridge regulates enzyme function. Nature. 2021 May 5. pii: 10.1038/s41586-021-03513-3. doi:, 10.1038/s41586-021-03513-3. PMID:33953398 doi:http://dx.doi.org/10.1038/s41586-021-03513-3
