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Structure of aldose reductase from Giardia lamblia
Giardia lamblia is an anaerobic aerotolerant eukaryotic parasite of the intestines. It is believed to have diverged early from eukarya during evolution and is thus lacking in many of the typical eukaryotic organelles and biochemical pathways. Most conspicuously, mitochondria and the associated machi...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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International Union of Crystallography
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3169411/ https://www.ncbi.nlm.nih.gov/pubmed/21904059 http://dx.doi.org/10.1107/S1744309111030879 |
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author | Ferrell, M. Abendroth, J. Zhang, Y. Sankaran, B. Edwards, T. E. Staker, B. L. Van Voorhis, W. C. Stewart, L. J. Myler, P. J. |
author_facet | Ferrell, M. Abendroth, J. Zhang, Y. Sankaran, B. Edwards, T. E. Staker, B. L. Van Voorhis, W. C. Stewart, L. J. Myler, P. J. |
author_sort | Ferrell, M. |
collection | PubMed |
description | Giardia lamblia is an anaerobic aerotolerant eukaryotic parasite of the intestines. It is believed to have diverged early from eukarya during evolution and is thus lacking in many of the typical eukaryotic organelles and biochemical pathways. Most conspicuously, mitochondria and the associated machinery of oxidative phosphorylation are absent; instead, energy is derived from substrate-level phosphorylation. Here, the 1.75 Å resolution crystal structure of G. lamblia aldose reductase heterologously expressed in Escherichia coli is reported. As in other oxidoreductases, G. lamblia aldose reductase adopts a TIM-barrel conformation with the NADP(+)-binding site located within the eight β-strands of the interior. |
format | Online Article Text |
id | pubmed-3169411 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
spelling | pubmed-31694112011-09-21 Structure of aldose reductase from Giardia lamblia Ferrell, M. Abendroth, J. Zhang, Y. Sankaran, B. Edwards, T. E. Staker, B. L. Van Voorhis, W. C. Stewart, L. J. Myler, P. J. Acta Crystallogr Sect F Struct Biol Cryst Commun Structural Communications Giardia lamblia is an anaerobic aerotolerant eukaryotic parasite of the intestines. It is believed to have diverged early from eukarya during evolution and is thus lacking in many of the typical eukaryotic organelles and biochemical pathways. Most conspicuously, mitochondria and the associated machinery of oxidative phosphorylation are absent; instead, energy is derived from substrate-level phosphorylation. Here, the 1.75 Å resolution crystal structure of G. lamblia aldose reductase heterologously expressed in Escherichia coli is reported. As in other oxidoreductases, G. lamblia aldose reductase adopts a TIM-barrel conformation with the NADP(+)-binding site located within the eight β-strands of the interior. International Union of Crystallography 2011-08-16 /pmc/articles/PMC3169411/ /pubmed/21904059 http://dx.doi.org/10.1107/S1744309111030879 Text en © Ferrell et al. 2011 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 Ferrell, M. Abendroth, J. Zhang, Y. Sankaran, B. Edwards, T. E. Staker, B. L. Van Voorhis, W. C. Stewart, L. J. Myler, P. J. Structure of aldose reductase from Giardia lamblia |
title | Structure of aldose reductase from Giardia lamblia
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title_full | Structure of aldose reductase from Giardia lamblia
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title_fullStr | Structure of aldose reductase from Giardia lamblia
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title_full_unstemmed | Structure of aldose reductase from Giardia lamblia
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title_short | Structure of aldose reductase from Giardia lamblia
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title_sort | structure of aldose reductase from giardia lamblia |
topic | Structural Communications |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3169411/ https://www.ncbi.nlm.nih.gov/pubmed/21904059 http://dx.doi.org/10.1107/S1744309111030879 |
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