4AG7

C. elegans glucosamine-6-phosphate N-acetyltransferase (GNA1): coenzyme A adduct

Summary for 4AG7

• Entry DOI: 10.2210/pdb4ag7/pdb
• Related: 4AG9
• Descriptor: GLUCOSAMINE-6-PHOSPHATE N-ACETYLTRANSFERASE, COENZYME A (3 entities in total)
• Functional Keywords: transferase
• Biological source: CAENORHABDITIS ELEGANS
• Total number of polymer chains: 2
• Total formula weight: 38497.46

Authors

Dorfmueller, H.C.,Fang, W.,Rao, F.V.,Blair, D.E.,Attrill, H.,Shepherd, S.M.,van Aalten, D.M.F. (deposition date: 2012-01-24, release date: 2012-07-25, Last modification date: 2024-11-13)

Primary citation

Dorfmueller, H.C.,Fang, W.,Rao, F.V.,Blair, D.E.,Attrill, H.,Van Aalten, D.M.F.
Structural and Biochemical Characterization of a Trapped Coenzyme a Adduct of Caenorhabditis Elegans Glucosamine-6-Phosphate N-Acetyltransferase 1.
Acta Crystallogr.,Sect.D, 68:1019-, 2012

PubMed Abstract: 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.

PubMed: 22868768
DOI: 10.1107/S0907444912019592

Experimental method

X-RAY DIFFRACTION (1.55 Å)