2008
DOI: 10.1074/jbc.m801017200
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Structural and Enzymatic Analysis of MshA from Corynebacterium glutamicum

Abstract: The glycosyltransferase termed MshA catalyzes the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to 1-Lmyo-inositol-1-phosphate in the first committed step of mycothiol biosynthesis. The structure of MshA from Corynebacterium glutamicum was determined both in the absence of substrates and in a complex with UDP and 1-L-myo-inositol-1-phosphate. MshA belongs to the GT-B structural family whose members have a two-domain structure with both domains exhibiting a Rossman-type fold. Binding of the donor… Show more

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Cited by 114 publications
(206 citation statements)
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“…The widening of the groove likely occurs by an outward movement of R-fold II, because such a conformational change has been observed in GtfA by us (Fig. 2B) and has been reported in other GT-B family members (38). In the GtfA/B dimer, GtfB binds to glycosylated substrate as strongly as in the absence of GtfA (a probably nonphysiological situation), consistent with R-fold II being unconstrained.…”
Section: Discussionsupporting
confidence: 54%
See 1 more Smart Citation
“…The widening of the groove likely occurs by an outward movement of R-fold II, because such a conformational change has been observed in GtfA by us (Fig. 2B) and has been reported in other GT-B family members (38). In the GtfA/B dimer, GtfB binds to glycosylated substrate as strongly as in the absence of GtfA (a probably nonphysiological situation), consistent with R-fold II being unconstrained.…”
Section: Discussionsupporting
confidence: 54%
“…In the tetramer, the conformation of GtfB is constrained by interaction with GtfA across interface II, allowing GtfB to bind nonglycosylated substrate. In the dimer, R-fold II of GtfB is unconstrained and could move outwards, as seen in other glycosyltransferases (38). The resulting relaxed conformation would allow interaction with substrate that already contains modified Ser/Thr residues.…”
Section: Resultsmentioning
confidence: 98%
“…However, co-crystallization experiments with UDP-GlcNAc, UDP-GlcN, or the natural substrate UDP-6-deoxy-AltdiNAc yielded a PseGHis 6 complex with bound UDP. Activity measurements in solution of PseGHis 6 with UDP-GlcNAc did not yield any significant activity, suggesting that the bound UDP observed in our structures is the result of either low UDP contamination of UDP-sugar preparations or spontaneous hydrolysis of the UDP-sugars either in the reservoir or upon storage (52).…”
Section: Resultsmentioning
confidence: 99%
“…Both models contain a C-terminal extension consisting of vector sequence from the C-terminal His 6 fusion tag, 275 Leu-GluHis 6 282 , which is ordered in the crystal structures. This C-terminal extension forms both direct and water-mediated H-bonds with the PseG molecule itself, as well as with a surfaceexposed cluster of negatively charged residues (Asp 30 , Asp 44 , Glu 52 , Glu 67 , and Glu 68 ) from a symmetry-related PseG molecule. Based on the crystal structures and analysis by size exclusion chromatography (result not shown), we surmise that the enzyme is a monomer.…”
Section: Resultsmentioning
confidence: 99%
“…Retaining-enzyme representatives, like WbdC, WbdB, and all but one domain of the WbdA homologs, possess a GT-B fold with a conserved EX 7 E motif. 6 Crystal structures place the EX 7 E motif within the catalytic site of the enzyme, and the consensus is that the motif is involved in binding of the nucleotide sugar donor (46,49,(51)(52)(53). Available structures show that the two Glu residues interact with hydrogen bond donors comprising the hydroxyl groups of the sugar moiety and ribose moieties of the nucleotide sugar, respectively.…”
Section: Volume 287 • Number 45 • November 2 2012mentioning
confidence: 99%