6th8

Reconstructing the Origins of the HemD-like fold

spinqualitylabelsall models 6th8 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6th8 is a 1 chain structure with sequence from Thermus thermophilus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function HEM4_PSEAE Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III. Publication Abstract from PubMed Evolutionary processes that led to the emergence of structured protein domains left footprints in the sequences of modern proteins. We searched for such hints employing state-of-the-art sequence analysis and found evidence that the HemD-like fold emerged from the flavodoxin-like fold through segment swap and gene duplication. To verify this hypothesis, we reverted these evolutionary steps experimentally, constructing a HemD-half that resulted in a protein with the canonical flavodoxin-like architecture. These results of fold reconstruction from the sequence of a different fold strongly support our hypothesis of common ancestry. It further illustrates the plasticity of modern proteins to form new folded proteins. Reconstructing the Remote Origins of a Fold Singleton from a Flavodoxin-Like Ancestor.,Toledo-Patino S, Chaubey M, Coles M, Hocker B Biochemistry. 2019 Nov 20. doi: 10.1021/acs.biochem.9b00900. PMID:31724394 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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