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

doi:10.1107/S1744309109010252

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 journal › Article › peer-review

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 language	English (US)
Pages (from-to)	435-439
Number of pages	5
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	65
Issue number	5
DOIs	https://doi.org/10.1107/S1744309109010252
State	Published - 2009
Externally published	Yes

Keywords

Acetyltransferases
Bifunctional enzymes
GlmU
Mycobacterium tuberculosis
Uridyltransferases

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Genetics
Condensed Matter Physics

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10.1107/S1744309109010252

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Structure of N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) from Mycobacterium tuberculosis in a cubic space group. / Verma, Sunil Kumar; Jaiswal, Mamta; Kumar, Neeraj et al.
In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 65, No. 5, 2009, p. 435-439.

Research output: Contribution to journal › Article › peer-review

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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 {\AA} 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.",

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AU - Verma, Sunil Kumar

AU - Jaiswal, Mamta

AU - Kumar, Neeraj

AU - Parikh, Amit

AU - Nandicoori, Vinay Kumar

AU - Prakash, Balaji

PY - 2009

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AB - 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.

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

Abstract

Keywords

ASJC Scopus subject areas

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