Crystal Structures and Enzyme Mechanisms of a Dual Fucose Mutarotase/Ribose Pyranase

Lee, Kwang Hoon; Ryu, Kyoung‐Seok; Kim, Min Sung; Suh, Hye Young; Ku, Bonsu; Song, Young Lan; Ko, Sunggeon; Lee, Weontae; Oh, Byung Ha

doi:10.1016/j.jmb.2009.06.022

Cited by 9 publications

(5 citation statements)

References 28 publications

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“…[259] The structure of the enzyme from E. coli (PDB 2WCV) was solved at ar esolution of 1.9 with l-fucose bound at the active site. [256] The enzyme crystallized as ad ecameric toroid and the electron density observed at the active site was consistent with the bindingo fb oth a-a nd b-l-fucose. Superposition of the structures of the bound anomers( Figure 4B)r eveals that, as with GalM, the binding orientationo ft he anomersf ollowst he superposition model.…”

Section: Fucose Mutarotase (Fucm)supporting

confidence: 59%

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Through the Looking Glass: Chiral Recognition of Substrates and Products at the Active Sites of Racemases and Epimerases

Bearne

2020

Chemistry A European J

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Unlike most enzymes, which exhibit stereospecific substrate binding, racemases and epimerases bind and catalyze the reversible interconversion of enantiomeric and epimeric pairs of substrates. Over the past 15 years, a growing number of racemase and epimerase structures have been solved, furnishing insights into the nature of chiral recognition of substrates by these enzymes. Those enzymes catalyzing stereoinversion of a carbon acid substrate through a direct 1,1‐proton transfer mechanism all bind their substrates in a mirror‐image packing orientation. This does not apply generally to racemases and epimerases that use other mechanisms, such as NADH‐dependent epimerases that employ a “flipping” mechanism. In general, polar groups are bound and fixed at the three binding determinants on the protein defining a pseudo‐mirror plane, while nonpolar groups may be mobile. The hydrogen atoms on each stereocenter are positioned antipodal with respect to the pseudo‐mirror plane, making a two‐base mechanism imperative. Recognition that mirror‐image packing is the common binding mode for enantiomeric or epimeric substrates of these enzymes should inform modelling/docking studies and protein engineering.

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Section: Fucose Mutarotase (Fucm)supporting

confidence: 59%

“…GalM from Lactococcus lactis (PDB 1L7K) are shown. [254] (B) b-l-Fucose( b-l-Fuc, blue) and a-l-fucose( a-l-Fuc, green)asb oundt oF ucM from Escherichia coli (PDB 2WCV)a re shown [256] (although only the a-anomer is present in PDB 2WCV,t he b-OH has been added in accord with Figure1bi n Ref. [256]]).…”

Section: Fucose Mutarotase (Fucm)mentioning

confidence: 99%

Through the Looking Glass: Chiral Recognition of Substrates and Products at the Active Sites of Racemases and Epimerases

Bearne

2020

Chemistry A European J

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“…Most residues of the sugar binding site were from one eFucU monomer. The neighboring subunit provided an additional histidine residue for sugar interaction, which was important for the enzymatic activity (Lee et al, 2009). The mouse homolog of eFucU (referred to as mFucU) also existed in dimeric form in crystals and the sugar binding site was formed by one subunit.…”

Section: The Ribose Binding Sitementioning

confidence: 99%

Crystal structure of Sa240: A ribose pyranase homolog with partial active site from Staphylococcus aureus

Zang

2011

Journal of Structural Biology

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“…Na análise proteômica dos isolados de EPECa BA320 (ALL), Ec292/84 (AA), 9100-83 (DA) e BA4013 (NA) foram identificadas proteínas com diferentes funções. Dentre essas proteínas foram identificadas: moléculas envolvidas no processo de regulação transcricional (H-NS), proteínas de membrana (OmpX), proteínas metabólicas (Usp), glicoproteínas (FucU) e proteínas transportadoras (MglB) associadas ao processo de funcionamento das adesinas fimbriais de E. coli (OTTO et al, 2004;NACHIN et al, 2005;HAN et al, 2007;TORRES et al, 2008;LEE et al, 2009).…”

Section: Discussionunclassified

“…Aparentemente as bactérias possuem formas sofisticadas para selecionar, conectar e infectar as células-alvo e durante esses eventos os principais protagonistas são os apêndices filamentosos secretores, as adesinas fimbriais e não-fimbrias (KROGFELT, 1991;EBEL et al, 1998;CLEARY et al, 2004, FRONZES;WAKSMAN, 2008). Entretanto, as enterobactérias ainda necessitam de uma complexa combinação de sinais físico-químicos (temperatura, pH, osmolaridade e nutrientes disponíveis) (EDWARDS; PUENTE, 1998), enzimas, metabólitos, proteínas estruturais e reguladores transcricionais (OTTO et al, 2004;NACHIN et al, 2005;HAN et al, 2007;TORRES et al, 2008;LEE et al, 2009). A combinação entre esses fatores podem prover as enterobactérias a capacidade de identificar o nicho apropriado e estimular a expressão dos genes fimbriais e não-fimbriais, resultando na ligação específica à célula hospedeira.…”

Section: Introductionunclassified

Adesinas fimbriais em Escherichia coli enteropatogênica atípica: prevalência e proteômica.

Nara¹

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Atypical enteropathogenic Escherichia coli (aEPEC) have emerged as a significant cause of pediatric diarrhea worldwide. Due to the absence of BFP fimbriae (bundle-forming pili), aEPEC are unable to develop the 3 h-localized adhesion pattern observed in typical EPEC. Since some aEPEC show the adherence phenotype observed for other pathotypes of E. coli, the aim of this study was to investigate, in aEPEC, the presence of adhesin genes found in other pathogenic E. coli and to analyze, by comparative proteomic analyses, the protein extracts isolated from aEPEC BA320 (localized-like), Ec292/84 (aggregative) and 9100-83 (diffuse) and BA4013 (non-adherent). Initially, transmission electron microscopy demonstrated the presence of different filamentous structures anchored to the surface in the four EPEC isolates. PCR analyses of aEPEC revealed the presence of the genes fimA, fimH, papA, ecpA, ldaH, pilS, daaC, sfpA, lpfA O113 and polymorphic variants (lpfA1 and lpfA2), which are also present in other pathotypes of E. coli. On the other hand, proteomic analyses of aEPEC extracts obtained with an Omnimixer and precipitated with ammonium sulfate, using 2D gel electrophoresis and LC-MS/MS, identified several proteins involved in different functional processes of bacteria, including proteins involved in the mechanism of bacterial adhesion, namely: a histone-like nucleoid structuring protein (H-NS), an outer membrane protein (OmpX), universal stress proteins (Usp), L-fucose mutarotase (FucU) and galactose-binding transport protein (MglB) associated with the action of adhesins of E. coli fimbriae. The protein extract also revealed "hypothetical" proteins, particularly a putative filamentous protein found in aEPEC with the phenotypes of localized-like, diffuse and aggregative adherence. Therefore, we conclude that the genes encoding type 1 fimbriae and ECP fimbriae are highly prevalent in aEPEC isolates, and that the proteins identified in the proteome of four aEPEC strains, which are related to different bacterial functions, can operate as protein complexes, directly or indirectly involved in adhesion processes.

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Crystal Structures and Enzyme Mechanisms of a Dual Fucose Mutarotase/Ribose Pyranase

Cited by 9 publications

References 28 publications

Through the Looking Glass: Chiral Recognition of Substrates and Products at the Active Sites of Racemases and Epimerases

Through the Looking Glass: Chiral Recognition of Substrates and Products at the Active Sites of Racemases and Epimerases

Crystal structure of Sa240: A ribose pyranase homolog with partial active site from Staphylococcus aureus

Adesinas fimbriais em Escherichia coli enteropatogênica atípica: prevalência e proteômica.

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