N-acetylglucosamine-1-phosphate uridyltransferase
From Proteopedia
(Difference between revisions)
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== 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 == | ||
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| + | 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 uracil binding pocket, GlcNAc interacting pocket and a lipophilic pocket <ref>PMID:18029420</ref>. | ||
</StructureSection> | </StructureSection> | ||
Revision as of 09:32, 13 April 2020
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3D structures of GlmU
Updated on 13-April-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
