7oey

Neisseria gonnorhoeae variant E93Q at 1.35 angstrom resolution

spinqualitylabelsall models 7oey, resolution 1.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7oey is a 2 chain structure with sequence from Neisseria gonorrhoeae FA 1090. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.35Å Ligands: CSO, GOL, NA, SIN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TAL_NEIG1 Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway (By similarity). Publication Abstract from PubMed We recently reported the discovery of a lysine-cysteine redox switch in proteins with a covalent nitrogen-oxygen-sulfur (NOS) bridge. Here, a systematic survey of the whole protein structure database discloses that NOS bridges are ubiquitous redox switches in proteins of all domains of life and are found in diverse structural motifs and chemical variants. In several instances, lysines are observed in simultaneous linkage with two cysteines, forming a sulfur-oxygen-nitrogen-oxygen-sulfur (SONOS) bridge with a trivalent nitrogen, which constitutes an unusual native branching cross-link. In many proteins, the NOS switch contains a functionally essential lysine with direct roles in enzyme catalysis or binding of substrates, DNA or effectors, linking lysine chemistry and redox biology as a regulatory principle. NOS/SONOS switches are frequently found in proteins from human and plant pathogens, including severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), and also in many human proteins with established roles in gene expression, redox signaling and homeostasis in physiological and pathophysiological conditions. Widespread occurrence of covalent lysine-cysteine redox switches in proteins.,Rabe von Pappenheim F, Wensien M, Ye J, Uranga J, Irisarri I, de Vries J, Funk LM, Mata RA, Tittmann K Nat Chem Biol. 2022 Feb 14. pii: 10.1038/s41589-021-00966-5. doi:, 10.1038/s41589-021-00966-5. PMID:35165445 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Transaldolase 3D structures

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