5zlk

Mutation in the trinuclear site of CotA-laccase: H493A mutant, PH 8.0

spinqualitylabelsall models 5zlk, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5zlk is a 1 chain structure with sequence from Bacillus subtilis subsp. subtilis str. 168. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.6Å Ligands: CU, EDO, GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function COTA_BACSU Involved in brown pigmentation during sporogenesis. Publication Abstract from PubMed In laccase, type-1 copper (Cu1) was connected to the trinuclear copper center (TNC) by the conserved Cys-His bridge. An allosteric coupling between the two redox sites has been reported; however, the molecular mechanism underlining the allosteric coupling is unknown. In this study, ligands of the two type 3 copper sites, including His491 and His493, in CotA were mutated to Cys or Ala. The crystal structures revealed that mutation at His491 and His493 caused rearrangement of the hydrogen bond network and geometric distortion of the TNC, which severely impaired the activities of mutants H493A, H493C and H491C. In addition, the change in TNC affected the hydrogen bonds around Cys492 in the mutants and led to the Cu1 was partially reduced. These results not only decipher the mechanism of allosteric coupling between Cu1 and TNC in laccase but also pave the curb for laccase protein engineering. Structural Insight into the Allosteric Coupling of Cu1 Site and Trinuclear Cu Cluster in CotA Laccase.,Xie T, Liu Z, Wang G Chembiochem. 2018 May 3. doi: 10.1002/cbic.201800236. PMID:29722464 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Laccase 3D structures

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