Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
GlmU is a bifunctional enzyme that catalyzes the final two steps in the biosynthesis of UDP-GlcNAc. Crystals of GlmU from Mycobacterium tuberculosis obtained using ammonium sulfate as a precipitant diffracted poorly (to 3.4 A resolution) and displayed an unusually high solvent content (>80%) with sparse crystal packing that resulted in large solvent channels. With one molecule per asymmetric unit, the monomers from three neighbouring asymmetric units related by the crystal threefold formed a biological trimer. Although this is the first report of the structure of GlmU determined in a cubic crystal form, the trimeric arrangement here is similar to that observed for other GlmU structures determined in hexagonal (H3, H32, P6(3)22) space groups.
Structure of N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) from Mycobacterium tuberculosis in a cubic space group.,Verma SK, Jaiswal M, Kumar N, Parikh A, Nandicoori VK, Prakash B Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 May 1;65(Pt, 5):435-9. Epub 2009 Apr 24. PMID:19407371[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Verma SK, Jaiswal M, Kumar N, Parikh A, Nandicoori VK, Prakash B. Structure of N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) from Mycobacterium tuberculosis in a cubic space group. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 May 1;65(Pt, 5):435-9. Epub 2009 Apr 24. PMID:19407371 doi:10.1107/S1744309109010252
