6k2h

structural characterization of mutated NreA protein in nitrate binding site from staphylococcus aureus.structural characterization of mutated NreA protein in nitrate binding site from staphylococcus aureus.

Structural highlights 6k2h is a 1 chain structure with sequence from Staphylococcus aureus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q2FVM5_STAA8 Publication Abstract from PubMed Staphylococcus aureus is an anaerobic facultative microorganism that features the NreABC system for nitrate respiration. NreB is the sensor histidine kinase that phosphorylates the response regulator NreC to stimulate the expression of target genes. NreA is a nitrate sensor which dissociates from NreB in the present of nitrate and relieves its inhibition on NreB. However, the molecular basis of how NreA regulate NreB remains unknown. In this study, we determined the crystal structures of nitrate-bound NreA from S. aureus (SaNreA/NO3(-)) and its apoNreA-like mutant SaNreAY(94A) in complex with ethanediol (SaNreA(Y94A)/EDO). Structural comparison reveals that the C-terminal loop in SaNreA/NO3(-) rearranges to an alpha-helix (alpha7) in SaNreA(Y94A)/EDO, which converts an acidic pocket on the surface to a positively charged region. This conformational change of SaNreA C-terminus might play a role in SaNreB binding. Structural insights into the conformational change of Staphylococcus aureus NreA at C-terminus.,Sangare L, Chen W, Wang C, Chen X, Wu M, Zhang X, Zang J Biotechnol Lett. 2020 Jan 22. pii: 10.1007/s10529-020-02807-2. doi:, 10.1007/s10529-020-02807-2. PMID:31970556 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 6k2h, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image