1w1z
From Proteopedia
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| - | | | + | {{STRUCTURE_1w1z| PDB=1w1z | SCENE= }} |
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'''STRUCTURE OF THE PLANT LIKE 5-AMINO LAEVULINIC ACID DEHYDRATASE FROM CHLOROBIUM VIBRIOFORME''' | '''STRUCTURE OF THE PLANT LIKE 5-AMINO LAEVULINIC ACID DEHYDRATASE FROM CHLOROBIUM VIBRIOFORME''' | ||
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[[Category: Shoolingin-Jordan, P.]] | [[Category: Shoolingin-Jordan, P.]] | ||
[[Category: Wood, S P.]] | [[Category: Wood, S P.]] | ||
| - | [[Category: | + | [[Category: Alad,porphyrin biosynthesis]] |
| - | [[Category: | + | [[Category: Heme biosynthesis]] |
| - | [[Category: | + | [[Category: Lyase]] |
| - | [[Category: | + | [[Category: Magnesium]] |
| - | [[Category: | + | [[Category: Tetrapyrrole biosynthesis]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:02:29 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 10:02, 3 May 2008
STRUCTURE OF THE PLANT LIKE 5-AMINO LAEVULINIC ACID DEHYDRATASE FROM CHLOROBIUM VIBRIOFORME
Overview
5-Aminolaevulinic acid dehydratase (ALAD), an early enzyme of the tetrapyrrole biosynthesis pathway, catalyses the dimerisation of 5-aminolaevulinic acid to form the pyrrole, porphobilinogen. ALAD from Chlorobium vibrioforme is shown to form a homo-octameric structure with 422 symmetry in which each subunit adopts a TIM-barrel fold with a 30 residue N-terminal arm extension. Pairs of monomers associate with their arms wrapped around each other. Four of these dimers interact principally via their arm regions to form octamers in which each active site is located on the surface. The active site contains two invariant lysine residues (200 and 253), one of which (Lys253) forms a Schiff base link with the bound substrate analogue, laevulinic acid. The carboxyl group of the laevulinic acid forms hydrogen bonds with the side-chains of Ser279 and Tyr318. The structure was examined to determine the location of the putative active-site magnesium ion, however, no evidence for the metal ion was found in the electron density map. This is in agreement with previous kinetic studies that have shown that magnesium stimulates but is not required for activity. A different site close to the active site flap, in which a putative magnesium ion is coordinated by a glutamate carboxyl and five solvent molecules may account for the stimulatory properties of magnesium ions on the enzyme.
About this Structure
1W1Z is a Single protein structure of sequence from Prosthecochloris vibrioformis. Full crystallographic information is available from OCA.
Reference
The X-ray structure of the plant like 5-aminolaevulinic acid dehydratase from Chlorobium vibrioforme complexed with the inhibitor laevulinic acid at 2.6 A resolution., Coates L, Beaven G, Erskine PT, Beale SI, Avissar YJ, Gill R, Mohammed F, Wood SP, Shoolingin-Jordan P, Cooper JB, J Mol Biol. 2004 Sep 10;342(2):563-70. PMID:15327955 Page seeded by OCA on Sat May 3 13:02:29 2008
Categories: Porphobilinogen synthase | Prosthecochloris vibrioformis | Single protein | Avissar, Y J. | Beale, S I. | Beaven, G. | Coates, L. | Cooper, J B. | Erskine, P T. | Gill, R. | Mohammed, F. | Shoolingin-Jordan, P. | Wood, S P. | Alad,porphyrin biosynthesis | Heme biosynthesis | Lyase | Magnesium | Tetrapyrrole biosynthesis
