6blm | pdb_00006blm

Crystal Structure of Native Fused 4-OT

spinqualitylabelsall models 6blm, resolution 1.49Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6blm is a 3 chain structure with sequence from Burkholderia lata. This structure supersedes the now removed PDB entry 5un4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.488Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q392K7_BURL3 Publication Abstract from PubMed The tautomerase superfamily (TSF) consists of more than 11,000 non-redundant sequences present throughout the biosphere. Characterized members have attracted much attention because of the unusual and key catalytic role of an N-terminal proline. These few characterized members catalyze a diverse range of chemical reactions, but the full scale of their chemical capabilities and biological functions remains unknown. To gain new insight into TSF structure-function relationships, we performed a global analysis of similarities across the entire superfamily and computed a sequence-similarity network to guide classification into distinct subgroups. Our results indicated that TSF members are found in all domains of life, with most being present in bacteria. The eukaryotic members of the cis-3- chloroacrylic acid dehalogenase subgroup are limited to fungal species, while the macrophagemigration inhibitory factor subgroup has wide eukaryotic representation (including mammals). Unexpectedly, we found that 346 TSF sequences lack Pro-1, of which 85% are present in the malonate semialdehyde decarboxylase subgroup. The computed network also enabled identification of similarity paths, namely sequences that link functionally diverse subgroups and exhibit transitional structural features that may help explain reaction divergence. A structure-guided comparison of these linker proteins identified conserved transitions between them, and kinetic analysis paralleled these observations. Phylogenetic reconstruction of the linker set was consistent with these findings. Our results also suggest that contemporary TSF members may have evolved from a short 4-oxalocrotonate tautomerase-like ancestor, followed by gene duplication and fusion. Our new linker-guided strategy can be used to enrich discovery of sequence/structure/function transitions in other enzyme superfamilies. A global view of structure-function relationships in the tautomerase superfamily.,Davidson R, Baas BJ, Akiva E, Holliday GL, Polacco BJ, LeVieux JA, Pullara CR, Zhang YJ, Whitman CP, Babbitt PC J Biol Chem. 2017 Nov 28. pii: M117.815340. doi: 10.1074/jbc.M117.815340. PMID:29184004 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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