N-acetylglucosamine-1-phosphate uridyltransferase
From Proteopedia
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| - | <StructureSection load='2v0j' size=' | + | <StructureSection load='2v0j' size='400' side='right' caption='GlmU complex with its reaction product UDP-GlcNAC, PEG, Mg++, So4, tetraethylene glycol and triethylene glycol (PDB code [[2v0j]])' scene='84/841078/Cv/1'> |
== Function == | == Function == | ||
| - | '''N-acetylglucosamine-1-phosphate uridyltransferase''' (GlmU | + | '''N-acetylglucosamine-1-phosphate uridyltransferase''' (GlmU) or '''bifunctional protein GlmU''' is a bifunctional acetyltransferase/uridyltransferase that catalyzes the formation of UDP-GlcNAc from glucosamine-1-phosphate (G1P)(<ref>PMID:19237750</ref>.) |
== Relevance == | == Relevance == | ||
| - | GlmU is essensial enzyme participating in the biosynthetic pathway for production of peptidoglycans which constitute the mycobacterial cell wall. Hence the inhibition of GlmU is a potential anti-tuberculosis drug target<ref>PMID: | + | GlmU is essensial enzyme participating in the biosynthetic pathway for production of peptidoglycans which constitute the mycobacterial cell wall. Hence the inhibition of GlmU is a potential anti-tuberculosis drug target<ref>PMID:318573680</ref>. |
== Structural highlights == | == Structural highlights == | ||
| + | |||
| + | The UDP-GlcNAc binds to GlmU in the enzyme's N-terminal domain and the majority of the key active site residues are highly conserved across the bacterial GlmU family. The 3D structure of the complex shows an exposed <scene name='84/841078/Cv/4'>uracil binding pocket</scene>, GlcNAc interacting pocket and a lipophilic pocket <ref>PMID:18029420</ref>. <scene name='84/841078/Cv/5'>Surface representation of the uracil binding pocket</scene>. | ||
</StructureSection> | </StructureSection> | ||
Current revision
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3D structures of GlmU
Updated on 29-December-2020
References
- ↑ 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
- ↑ . PMID:318573680
- ↑ Mochalkin I, Lightle S, Zhu Y, Ohren JF, Spessard C, Chirgadze NY, Banotai C, Melnick M, McDowell L. Characterization of substrate binding and catalysis in the potential antibacterial target N-acetylglucosamine-1-phosphate uridyltransferase (GlmU). Protein Sci. 2007 Dec;16(12):2657-66. PMID:18029420 doi:http://dx.doi.org/16/12/2657
