4g87 | pdb_00004g87

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Template:STRUCTURE 4g87

Crystal structure of GLMU from Mycobacterium tuberculosis snapshot 1

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

4g87 is a 1 chain structure with sequence from Mycobacterium tuberculosis h37rv. Full crystallographic information is available from OCA.

Reference

  1. 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

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