4u28

Crystal structure of apo Phosphoribosyl isomerase A from Streptomyces sviceus ATCC 29083

spinqualitylabelsall models 4u28, resolution 1.33Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4u28 is a 1 chain structure with sequence from Streptomyces sviceus ATCC 29083. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.33Å Ligands: MSE, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B5I4P8_STRX2 Involved in both the histidine and tryptophan biosynthetic pathways.[HAMAP-Rule:MF_01014] Publication Abstract from PubMed We investigate the evolution of co-occurring analogous enzymes involved in L-tryptophan and L-histidine biosynthesis in Actinobacteria Phylogenetic analysis of trpF homologues, a missing gene in certain clades of this lineage whose absence is complemented by a dual-substrate HisA homologue, termed PriA, found that they fall into three categories: (i) trpF-1, an L-tryptophan biosynthetic gene horizontally acquired by certain Corynebacterium species; (ii) trpF-2, a paralogue known to be involved in synthesizing a pyrrolopyrrole moiety and (iii) trpF-3, a variable non-conserved orthologue of trpF-1 We previously investigated the effect of trpF-1 upon the evolution of PriA substrate specificity, but nothing is known about the relationship between trpF-3 and priA After in vitro steady-state enzyme kinetics we found that trpF-3 encodes a phosphoribosyl anthranilate isomerase. However, mutation of this gene in Streptomyces sviceus did not lead to auxothrophy, as expected from the biosynthetic role of trpF-1 Biochemical characterization of a dozen co-occurring TrpF-2 or TrpF-3, with PriA homologues, explained the prototrophic phenotype, and unveiled an enzyme activity trade-off between TrpF and PriA. X-ray structural analysis suggests that the function of these PriA homologues is mediated by non-conserved mutations in the flexible L5 loop, which may be responsible for different substrate affinities. Thus, the PriA homologues that co-occur with TrpF-3 represent a novel enzyme family, termed PriB, which evolved in response to PRA isomerase activity. The characterization of co-occurring enzymes provides insights into the influence of functional redundancy on the evolution of enzyme function, which could be useful for enzyme functional annotation. Co-occurrence of analogous enzymes determines evolution of a novel (betaalpha)8-isomerase sub-family after non-conserved mutations in flexible loop.,Verduzco-Castro EA, Michalska K, Endres M, Juarez-Vazquez AL, Noda-Garcia L, Chang C, Henry CS, Babnigg G, Joachimiak A, Barona-Gomez F Biochem J. 2016 May 1;473(9):1141-52. doi: 10.1042/BJ20151271. Epub 2016 Feb 29. PMID:26929404 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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