4ag7: Difference between revisions
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==C. elegans glucosamine-6-phosphate N-acetyltransferase (GNA1): coenzyme A adduct== | ==C. elegans glucosamine-6-phosphate N-acetyltransferase (GNA1): coenzyme A adduct== | ||
<StructureSection load='4ag7' size='340' side='right' caption='[[4ag7]], [[Resolution|resolution]] 1.55Å' scene=''> | <StructureSection load='4ag7' size='340' side='right'caption='[[4ag7]], [[Resolution|resolution]] 1.55Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ag7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Caeel Caeel]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AG7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AG7 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4ag7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Caeel Caeel]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AG7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AG7 FirstGlance]. <br> | ||
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[[Category: Caeel]] | [[Category: Caeel]] | ||
[[Category: Glucosamine-phosphate N-acetyltransferase]] | [[Category: Glucosamine-phosphate N-acetyltransferase]] | ||
[[Category: Aalten, D M.F | [[Category: Aalten, D M.F van]] | ||
[[Category: Attrill, H]] | [[Category: Attrill, H]] | ||
[[Category: Blair, D E]] | [[Category: Blair, D E]] | ||
Revision as of 11:50, 6 March 2019
C. elegans glucosamine-6-phosphate N-acetyltransferase (GNA1): coenzyme A adductC. elegans glucosamine-6-phosphate N-acetyltransferase (GNA1): coenzyme A adduct
Structural highlights
Publication Abstract from PubMedGlucosamine-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. Structural and biochemical characterization of a trapped coenzyme A adduct of Caenorhabditis elegans glucosamine-6-phosphate N-acetyltransferase 1.,Dorfmueller HC, Fang W, Rao FV, Blair DE, Attrill H, van Aalten DM Acta Crystallogr D Biol Crystallogr. 2012 Aug;68(Pt 8):1019-29. Epub 2012 Jul 17. PMID:22868768[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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