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Structural insights into the monosaccharide specificity of Escherichia coli rhamnose mutarotase.

Ryu KS, Kim JI, Cho SJ, Park D, Park C, Cheong HK, Lee JO, Choi BS
J Mol Biol 349 153-62 (2005)
Cited: 17 times
EuropePMC logo PMID: 15876375

Abstract

The crystal structure of Escherichia coli rhamnose mutarotase (YiiL) is completely different from the previously reported structures of the Lactococcus lactis galactose mutarotase and the Bacillus subtilis RbsD (pyranase). YiiL exists as a locally asymmetric dimer, which is stabilized by an intermolecular beta-sheet, various hydrophobic interactions, and a cation-pi interaction with a salt-bridge. The protein folds of YiiL are similar to those of a Streptomyces coelicolor mono-oxygenase and a hypothetical Arabidopsis thaliana protein At3g17210. By assaying the enzymatic activity of six active-site mutants and by comparing the crystal structure-derived active site conformations of YiiL, RbsD, and a galactose mutarotase, we were able to define the amino acid residues required for catalysis and suggest a possible catalytic mechanism for YiiL. Although the active-site amino acid residues of YiiL (His, Tyr, and Trp) differ greatly from those of galactose mutarotase (His, Glu, and Asp), their geometries, which determine the structures of the preferred monosaccharide substrates, are conserved. In addition, the in vivo function of YiiL was assessed by constructing a mutant E.coli strain that carries a yiiL deletion. The presence of the yiiL gene is critical for efficient cell growth only when concentrations of l-rhamnose are limited.

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  2. Comparative genomics and functional analysis of rhamnose catabolic pathways and regulons in bacteria. Rodionova IA, Li X, Thiel V, Stolyar S, Stanton K, Fredrickson JK, Bryant DA, Osterman AL, Best AA, Rodionov DA. Front Microbiol 4 407 (2013)
  3. Partitioning of functional and taxonomic diversity in surface-associated microbial communities. Roth-Schulze AJ, Zozaya-Valdés E, Steinberg PD, Thomas T. Environ Microbiol 18 4391-4402 (2016)
  4. Crystal structure of YihS in complex with D-mannose: structural annotation of Escherichia coli and Salmonella enterica yihS-encoded proteins to an aldose-ketose isomerase. Itoh T, Mikami B, Hashimoto W, Murata K. J Mol Biol 377 1443-1459 (2008)
  5. Structure-based functional annotation: yeast ymr099c codes for a D-hexose-6-phosphate mutarotase. Graille M, Baltaze JP, Leulliot N, Liger D, Quevillon-Cheruel S, van Tilbeurgh H. J Biol Chem 281 30175-30185 (2006)
  6. Regulation of the rhaEWRBMA Operon Involved in l-Rhamnose Catabolism through Two Transcriptional Factors, RhaR and CcpA, in Bacillus subtilis. Hirooka K, Kodoi Y, Satomura T, Fujita Y. J Bacteriol 198 830-845 (2015)
  7. RhaU of Rhizobium leguminosarum is a rhamnose mutarotase. Richardson JS, Carpena X, Switala J, Perez-Luque R, Donald LJ, Loewen PC, Oresnik IJ. J Bacteriol 190 2903-2910 (2008)
  8. Cloning and characterization of a rhamnose isomerase from Bacillus halodurans. Prabhu P, Doan TT, Jeya M, Kang LW, Lee JK. Appl Microbiol Biotechnol 89 635-644 (2011)
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  12. Crystal structures and enzyme mechanisms of a dual fucose mutarotase/ribose pyranase. Lee KH, Ryu KS, Kim MS, Suh HY, Ku B, Song YL, Ko S, Lee W, Oh BH. J Mol Biol 391 178-191 (2009)
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  14. Anaerobic Growth of Listeria monocytogenes on Rhamnose Is Stimulated by Vitamin B12 and Bacterial Microcompartment-Dependent 1,2-Propanediol Utilization. Zeng Z, Li S, Boeren S, Smid EJ, Notebaart RA, Abee T. mSphere 6 e0043421 (2021)
  15. Global population structure, genomic diversity and carbohydrate fermentation characteristics of clonal complex 119 (CC119), an understudied Shiga toxin-producing E. coli (STEC) lineage including O165:H25 and O172:H25. Nakamura K, Seto K, Lee K, Ooka T, Gotoh Y, Taniguchi I, Ogura Y, Mainil JG, Piérard D, Harada T, Etoh Y, Ueda S, Hamasaki M, Isobe J, Kimata K, Narimatsu H, Yatsuyanagi J, Ohnishi M, Iyoda S, Hayashi T. Microb Genom 9 (2023)


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