3FOQ

Crystal structure of N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) from Mycobacterium tuberculosis in a cubic space group.

Summary for 3FOQ

• Entry DOI: 10.2210/pdb3foq/pdb
• Related: 3DK5
• Descriptor: Bifunctional protein glmU, SULFATE ION (2 entities in total)
• Functional Keywords: acetyltransferase, bifunctional, pyrophosphorylase, rossmann-like fold, left-handed-beta-helix, trimer, acyltransferase, cell shape, cell wall biogenesis/degradation, cytoplasm, magnesium, metal-binding, multifunctional enzyme, nucleotidyltransferase, peptidoglycan synthesis, transferase
• Biological source: Mycobacterium tuberculosis
• Cellular location: Cytoplasm (By similarity): P96382
• Total number of polymer chains: 1
• Total formula weight: 53111.23

Authors

Verma, S.K.,Prakash, B. (deposition date: 2008-12-31, release date: 2009-06-09, Last modification date: 2024-03-20)

Primary citation

Verma, S.K.,Jaiswal, M.,Kumar, N.,Parikh, A.,Nandicoori, V.K.,Prakash, B.
Structure of N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) from Mycobacterium tuberculosis in a cubic space group.
Acta Crystallogr.,Sect.F, 65:435-439, 2009

PubMed Abstract: 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.

PubMed: 19407371
DOI: 10.1107/S1744309109010252

Experimental method

X-RAY DIFFRACTION (3.41 Å)