N-acetylglucosamine-1-phosphate uridyltransferase
From Proteopedia
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== 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 uracil binding pocket, GlcNAc interacting pocket and a lipophilic pocket <ref>PMID:18029420</ref>. | + | 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/3'>uracil binding pocket</scene>, GlcNAc interacting pocket and a lipophilic pocket <ref>PMID:18029420</ref>. |
</StructureSection> | </StructureSection> | ||
Revision as of 14:40, 11 May 2020
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3D structures of GlmU
Updated on 11-May-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
