1AW8
PYRUVOYL DEPENDENT ASPARTATE DECARBOXYLASE
Summary for 1AW8
| Entry DOI | 10.2210/pdb1aw8/pdb |
| Descriptor | L-ASPARTATE-ALPHA-DECARBOXYLASE (3 entities in total) |
| Functional Keywords | decarboxylase, pantothenate pathway, lyase, protein self-processing |
| Biological source | Escherichia coli More |
| Cellular location | Cytoplasm : P0A790 P0A790 |
| Total number of polymer chains | 4 |
| Total formula weight | 25428.64 |
| Authors | Albert, A.,Dhanaraj, V.,Genschel, U.,Khan, G.,Ramjee, M.K.,Pulido, R.,Sybanda, B.L.,von Delf, F.,Witty, M.,Blundell, T.L.,Smith, A.G.,Abell, C. (deposition date: 1997-10-12, release date: 1998-04-29, Last modification date: 2024-10-23) |
| Primary citation | Albert, A.,Dhanaraj, V.,Genschel, U.,Khan, G.,Ramjee, M.K.,Pulido, R.,Sibanda, B.L.,von Delft, F.,Witty, M.,Blundell, T.L.,Smith, A.G.,Abell, C. Crystal structure of aspartate decarboxylase at 2.2 A resolution provides evidence for an ester in protein self-processing. Nat.Struct.Biol., 5:289-293, 1998 Cited by PubMed Abstract: 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. PubMed: 9546220DOI: 10.1038/nsb0498-289 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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