Journal
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY
Volume 68, Issue -, Pages 1019-1029Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S0907444912019592
Keywords
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Funding
- MRC [G0900138/90614]
- FEBS
- Marie Curie IRG grant
- Wellcome Trust [WT087590MA]
- Medical Research Council [G0900138] Funding Source: researchfish
- MRC [G0900138] Funding Source: UKRI
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Glucosamine-6-phosphate N-acetyltransferase 1 (GNA1) produces GlcNAc-6-phosphate from GlcN-6-phosphate and acetyl coenzyme A. Early mercury-labelling experiments implicated a conserved cysteine in the reaction mechanism, whereas recent structural data appear to support a mechanism in which this cysteine plays no role. Here, two crystal structures of Caenorhabditis elegans GNA1 are reported, revealing an unusual covalent complex between this cysteine and the coenzyme A product. Mass-spectrometric and reduction studies showed that this inactive covalent complex can be reactivated through reduction, yet mutagenesis of the cysteine supports a previously reported bi-bi mechanism. The data unify the apparently contradictory earlier reports on the role of a cysteine in the GNA1 active site.
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