Crystal structure of aspartate decarboxylase at 2.2 A resolution provides evidence for an ester in protein self-processing.
The structure of L-aspartate-alpha-decarboxylase from E. coli has been determined at 2.2 A resolution. The enzyme is a tetramer with pseudofour-fold rotational symmetry. The subunits are six-stranded beta-barrels capped by small alpha-helices at each end. The active sites are located between adjacen...
| Main Authors: | , , , , , , , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
1998
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| _version_ | 1797057336473288704 |
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| author | Albert, A Dhanaraj, V Genschel, U Khan, G Ramjee, M Pulido, R Sibanda, B von Delft, F Witty, M Blundell, T Smith, A Abell, C |
| author_facet | Albert, A Dhanaraj, V Genschel, U Khan, G Ramjee, M Pulido, R Sibanda, B von Delft, F Witty, M Blundell, T Smith, A Abell, C |
| author_sort | Albert, A |
| collection | OXFORD |
| description | The structure of L-aspartate-alpha-decarboxylase from E. coli has been determined at 2.2 A resolution. The enzyme is a tetramer with pseudofour-fold rotational symmetry. The subunits are six-stranded beta-barrels capped by small alpha-helices at each end. The active sites are located between adjacent subunits. The electron density provides evidence for catalytic pyruvoyl groups at three active sites and an ester at the fourth. The ester is an intermediate in the autocatalytic self-processing leading to formation of the pyruvoyl group. This unprecedented structure provides novel insights into the general phenomenon of protein processing. |
| first_indexed | 2024-03-06T19:34:51Z |
| format | Journal article |
| id | oxford-uuid:1eae8b3a-bde7-4dee-ae69-2b2b584fc69a |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T19:34:51Z |
| publishDate | 1998 |
| record_format | dspace |
| spelling | oxford-uuid:1eae8b3a-bde7-4dee-ae69-2b2b584fc69a2022-03-26T11:17:46ZCrystal structure of aspartate decarboxylase at 2.2 A resolution provides evidence for an ester in protein self-processing.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:1eae8b3a-bde7-4dee-ae69-2b2b584fc69aEnglishSymplectic Elements at Oxford1998Albert, ADhanaraj, VGenschel, UKhan, GRamjee, MPulido, RSibanda, Bvon Delft, FWitty, MBlundell, TSmith, AAbell, CThe structure of L-aspartate-alpha-decarboxylase from E. coli has been determined at 2.2 A resolution. The enzyme is a tetramer with pseudofour-fold rotational symmetry. The subunits are six-stranded beta-barrels capped by small alpha-helices at each end. The active sites are located between adjacent subunits. The electron density provides evidence for catalytic pyruvoyl groups at three active sites and an ester at the fourth. The ester is an intermediate in the autocatalytic self-processing leading to formation of the pyruvoyl group. This unprecedented structure provides novel insights into the general phenomenon of protein processing. |
| spellingShingle | Albert, A Dhanaraj, V Genschel, U Khan, G Ramjee, M Pulido, R Sibanda, B von Delft, F Witty, M Blundell, T Smith, A Abell, C Crystal structure of aspartate decarboxylase at 2.2 A resolution provides evidence for an ester in protein self-processing. |
| title | Crystal structure of aspartate decarboxylase at 2.2 A resolution provides evidence for an ester in protein self-processing. |
| title_full | Crystal structure of aspartate decarboxylase at 2.2 A resolution provides evidence for an ester in protein self-processing. |
| title_fullStr | Crystal structure of aspartate decarboxylase at 2.2 A resolution provides evidence for an ester in protein self-processing. |
| title_full_unstemmed | Crystal structure of aspartate decarboxylase at 2.2 A resolution provides evidence for an ester in protein self-processing. |
| title_short | Crystal structure of aspartate decarboxylase at 2.2 A resolution provides evidence for an ester in protein self-processing. |
| title_sort | crystal structure of aspartate decarboxylase at 2 2 a resolution provides evidence for an ester in protein self processing |
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