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Structure of N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) from Mycobacterium tuberculosis in a cubic space group
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...
Autores principales: | , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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International Union of Crystallography
2009
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2675579/ https://www.ncbi.nlm.nih.gov/pubmed/19407371 http://dx.doi.org/10.1107/S1744309109010252 |
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author | Verma, Sunil Kumar Jaiswal, Mamta Kumar, Neeraj Parikh, Amit Nandicoori, Vinay Kumar Prakash, Balaji |
author_facet | Verma, Sunil Kumar Jaiswal, Mamta Kumar, Neeraj Parikh, Amit Nandicoori, Vinay Kumar Prakash, Balaji |
author_sort | Verma, Sunil Kumar |
collection | PubMed |
description | 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, P6(3)22) space groups. |
format | Text |
id | pubmed-2675579 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2009 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
spelling | pubmed-26755792009-05-06 Structure of N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) from Mycobacterium tuberculosis in a cubic space group Verma, Sunil Kumar Jaiswal, Mamta Kumar, Neeraj Parikh, Amit Nandicoori, Vinay Kumar Prakash, Balaji Acta Crystallogr Sect F Struct Biol Cryst Commun Structural Communications 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, P6(3)22) space groups. International Union of Crystallography 2009-04-24 /pmc/articles/PMC2675579/ /pubmed/19407371 http://dx.doi.org/10.1107/S1744309109010252 Text en © Verma et al. 2009 http://creativecommons.org/licenses/by/2.0/uk/ This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited. |
spellingShingle | Structural Communications Verma, Sunil Kumar Jaiswal, Mamta Kumar, Neeraj Parikh, Amit Nandicoori, Vinay Kumar Prakash, Balaji Structure of N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) from Mycobacterium tuberculosis in a cubic space group |
title | Structure of N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) from Mycobacterium tuberculosis in a cubic space group |
title_full | Structure of N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) from Mycobacterium tuberculosis in a cubic space group |
title_fullStr | Structure of N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) from Mycobacterium tuberculosis in a cubic space group |
title_full_unstemmed | Structure of N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) from Mycobacterium tuberculosis in a cubic space group |
title_short | Structure of N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) from Mycobacterium tuberculosis in a cubic space group |
title_sort | structure of n-acetylglucosamine-1-phosphate uridyltransferase (glmu) from mycobacterium tuberculosis in a cubic space group |
topic | Structural Communications |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2675579/ https://www.ncbi.nlm.nih.gov/pubmed/19407371 http://dx.doi.org/10.1107/S1744309109010252 |
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