4hcq

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Template:STRUCTURE 4hcq

Contents 1 Crystal structure of GLMU from mycobacterium tuberculosis in complex with glucosamine-1-phosphate 2 Function 3 About this Structure 4 Reference

Crystal structure of GLMU from mycobacterium tuberculosis in complex with glucosamine-1-phosphate

Template:ABSTRACT PUBMED 23485416

Function

[GLMU_MYCTU] Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.^{[1] [2]}

About this Structure

4hcq is a 1 chain structure with sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

Reference

• Jagtap PK, Verma SK, Vithani N, Bais VS, Prakash B. Crystal structures identify an atypical two-metal-ion mechanism for uridyltransfer in GlmU: its significance to sugar nucleotidyl transferases. J Mol Biol. 2013 May 27;425(10):1745-59. doi: 10.1016/j.jmb.2013.02.019. Epub, 2013 Feb 26. PMID:23485416 doi:10.1016/j.jmb.2013.02.019

1. ↑ Zhang Z, Bulloch EM, Bunker RD, Baker EN, Squire CJ. Structure and function of GlmU from Mycobacterium tuberculosis. Acta Crystallogr D Biol Crystallogr. 2009 Mar;65(Pt 3):275-83. Epub 2009, Feb 20. PMID:19237750 doi:10.1107/S0907444909001036
2. ↑ Parikh A, Verma SK, Khan S, Prakash B, Nandicoori VK. PknB-mediated phosphorylation of a novel substrate, N-acetylglucosamine-1-phosphate uridyltransferase, modulates its acetyltransferase activity. J Mol Biol. 2009 Feb 20;386(2):451-64. Epub 2008 Dec 24. PMID:19121323 doi:10.1016/j.jmb.2008.12.031