Crystal structure of a Pseudomonas malonate decarboxylase holoenzyme hetero-tetramer
Some aerobic bacteria contain a biotin-independent malonate decarboxylase (MDC), which allows them to use malonate as the sole carbon source. Here, the authors present the crystal structure of a Pseudomonas MDC and give insights into its catalytic mechanism and function.
Guardado en:
Autores principales: | , , , , , , |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2017
|
Materias: | |
Acceso en línea: | https://doaj.org/article/71d0bb1020194c1092eae9c19f66e386 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
id |
oai:doaj.org-article:71d0bb1020194c1092eae9c19f66e386 |
---|---|
record_format |
dspace |
spelling |
oai:doaj.org-article:71d0bb1020194c1092eae9c19f66e3862021-12-02T10:48:18ZCrystal structure of a Pseudomonas malonate decarboxylase holoenzyme hetero-tetramer10.1038/s41467-017-00233-z2041-1723https://doaj.org/article/71d0bb1020194c1092eae9c19f66e3862017-07-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-00233-zhttps://doaj.org/toc/2041-1723Some aerobic bacteria contain a biotin-independent malonate decarboxylase (MDC), which allows them to use malonate as the sole carbon source. Here, the authors present the crystal structure of a Pseudomonas MDC and give insights into its catalytic mechanism and function.Riyaz MaderbocusBlanche L. FieldsKeith HamiltonShukun LuoTimothy H. TranLars E. P. DietrichLiang TongNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-12 (2017) |
institution |
DOAJ |
collection |
DOAJ |
language |
EN |
topic |
Science Q |
spellingShingle |
Science Q Riyaz Maderbocus Blanche L. Fields Keith Hamilton Shukun Luo Timothy H. Tran Lars E. P. Dietrich Liang Tong Crystal structure of a Pseudomonas malonate decarboxylase holoenzyme hetero-tetramer |
description |
Some aerobic bacteria contain a biotin-independent malonate decarboxylase (MDC), which allows them to use malonate as the sole carbon source. Here, the authors present the crystal structure of a Pseudomonas MDC and give insights into its catalytic mechanism and function. |
format |
article |
author |
Riyaz Maderbocus Blanche L. Fields Keith Hamilton Shukun Luo Timothy H. Tran Lars E. P. Dietrich Liang Tong |
author_facet |
Riyaz Maderbocus Blanche L. Fields Keith Hamilton Shukun Luo Timothy H. Tran Lars E. P. Dietrich Liang Tong |
author_sort |
Riyaz Maderbocus |
title |
Crystal structure of a Pseudomonas malonate decarboxylase holoenzyme hetero-tetramer |
title_short |
Crystal structure of a Pseudomonas malonate decarboxylase holoenzyme hetero-tetramer |
title_full |
Crystal structure of a Pseudomonas malonate decarboxylase holoenzyme hetero-tetramer |
title_fullStr |
Crystal structure of a Pseudomonas malonate decarboxylase holoenzyme hetero-tetramer |
title_full_unstemmed |
Crystal structure of a Pseudomonas malonate decarboxylase holoenzyme hetero-tetramer |
title_sort |
crystal structure of a pseudomonas malonate decarboxylase holoenzyme hetero-tetramer |
publisher |
Nature Portfolio |
publishDate |
2017 |
url |
https://doaj.org/article/71d0bb1020194c1092eae9c19f66e386 |
work_keys_str_mv |
AT riyazmaderbocus crystalstructureofapseudomonasmalonatedecarboxylaseholoenzymeheterotetramer AT blanchelfields crystalstructureofapseudomonasmalonatedecarboxylaseholoenzymeheterotetramer AT keithhamilton crystalstructureofapseudomonasmalonatedecarboxylaseholoenzymeheterotetramer AT shukunluo crystalstructureofapseudomonasmalonatedecarboxylaseholoenzymeheterotetramer AT timothyhtran crystalstructureofapseudomonasmalonatedecarboxylaseholoenzymeheterotetramer AT larsepdietrich crystalstructureofapseudomonasmalonatedecarboxylaseholoenzymeheterotetramer AT liangtong crystalstructureofapseudomonasmalonatedecarboxylaseholoenzymeheterotetramer |
_version_ |
1718396655033647104 |