ArticleEMBO reports2005
Two-fold repeated (betaalpha)4 half-barrels may provide a molecular tool for dual substrate specificity.
Article in EMBO reports, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Article
- Endoglucanase activity at a second site inFEBS open bio · 2017Article
- Co-occurrence of analogous enzymes determines evolution of a novel (βα)8-isomerase sub-family after non-conserved mutations in flexible loop.The Biochemical journal · 2016Article
- Long-Term Persistence of Bi-functionality Contributes to the Robustness of Microbial Life through Exaptation.PLoS genetics · 2016Article
- Two-step Ligand Binding in a (βα)8 Barrel Enzyme: SUBSTRATE-BOUND STRUCTURES SHED NEW LIGHT ON THE CATALYTIC CYCLE OF HisA.The Journal of biological chemistry · 2015Article
- Insights into the evolution of enzyme substrate promiscuity after the discovery of (βα)₈ isomerase evolutionary intermediates from a diverse metagenome.BMC evolutionary biology · 2015Article
- Bisubstrate specificity in histidine/tryptophan biosynthesis isomerase from Mycobacterium tuberculosis by active site metamorphosis.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Detecting internally symmetric protein structures.BMC bioinformatics · 2010Article
- Identification and analysis of residues contained on beta --> alpha loops of the dual-substrate (beta alpha)8 phosphoribosyl isomerase A specific for its phosphoribosyl anthranilate isomerase activity.Protein science : a publication of the Protein Society · 2010Article
- Establishing wild-type levels of catalytic activity on natural and artificial (beta alpha)8-barrel protein scaffolds.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Enzyme-driven speciation: crystallizing Archaea via lipid capture.Journal of molecular evolution · 2007Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Some bacterial genomes contain an incomplete set of genes encoding phosphoribosyl isomerases, raising the question of whether there exists broadened substrate specificity for the missing gene products. To investigate the underlying molecular principles of this hypothesis, we have determined the crystal structure of the bifunctional enzyme PriA from Streptomyces coelicolor at 1.8 A resolution. It consists of a (betaalpha)(8)-barrel fold that is assembled by two symmetric (betaalpha)(4) half-barrels. The structure shows how its active site may catalyse the isomerization reactions of two different substrates, and we provide a plausible model of how the smaller of the two substrates could be bound in two different orientations. Our findings expand the half-barrel ancestor concept by demonstrating that symmetry-related half-barrels could provide a smart solution to cope with dual substrate specificity. The data may help to unravel molecular rationales regarding how organisms with miniature genomes can keep central biological pathways functional.
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