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

Sunil Kumar Verma, Mamta Jaiswal, Neeraj Kumar, Amit Parikh, Vinay Kumar Nandicoori, Balaji Prakash

Research output: Contribution to journalArticle

12 Scopus citations

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 Å 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, P6322) space groups.

Original languageEnglish (US)
Pages (from-to)435-439
Number of pages5
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume65
Issue number5
DOIs
StatePublished - Jun 22 2009

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Keywords

  • Acetyltransferases
  • Bifunctional enzymes
  • GlmU
  • Mycobacterium tuberculosis
  • Uridyltransferases

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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