6cun

Engineered Cytochrome c from Rhodothermus marinus (Rma TDE) bound to carbene intermediate (1-ethoxy-1-oxopropan-2-ylidene)

spinqualitylabelsall models 6cun, resolution 1.29Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6cun is a 1 chain structure with sequence from Rhodothermus marinus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.29Å Ligands: CA1, HEC Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B3FQS5_RHOMR Publication Abstract from PubMed Recently, heme proteins have been discovered and engineered by directed evolution to catalyze chemical transformations that are biochemically unprecedented. Many of these nonnatural enzyme-catalyzed reactions are assumed to proceed through a catalytic iron porphyrin carbene (IPC) intermediate, although this intermediate has never been observed in a protein. Using crystallographic, spectroscopic, and computational methods, we have captured and studied a catalytic IPC intermediate in the active site of an enzyme derived from thermostable Rhodothermus marinus (Rma) cytochrome c High-resolution crystal structures and computational methods reveal how directed evolution created an active site for carbene transfer in an electron transfer protein and how the laboratory-evolved enzyme achieves perfect carbene transfer stereoselectivity by holding the catalytic IPC in a single orientation. We also discovered that the IPC in Rma cytochrome c has a singlet ground electronic state and that the protein environment uses geometrical constraints and noncovalent interactions to influence different IPC electronic states. This information helps us to understand the impressive reactivity and selectivity of carbene transfer enzymes and offers insights that will guide and inspire future engineering efforts. Catalytic iron-carbene intermediate revealed in a cytochrome c carbene transferase.,Lewis RD, Garcia-Borras M, Chalkley MJ, Buller AR, Houk KN, Kan SBJ, Arnold FH Proc Natl Acad Sci U S A. 2018 Jun 26. pii: 1807027115. doi:, 10.1073/pnas.1807027115. PMID:29946033 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cytochrome C 3D structures

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