1w31
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The X-ray structure of the enzyme 5-aminolaevulinic acid dehydratase | + | The X-ray structure of the enzyme 5-aminolaevulinic acid dehydratase (ALAD) from yeast complexed with the competitive inhibitor 5-hydroxylaevulinic acid has been determined at a resolution of 1.9 A. The structure shows that the inhibitor is bound by a Schiff-base link to one of the invariant active-site lysine residues (Lys263). The inhibitor appears to bind in two well defined conformations and the interactions made by it suggest that it is a very close analogue of the substrate 5-aminolaevulinic acid (ALA). |
==About this Structure== | ==About this Structure== | ||
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[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Beaven, G | + | [[Category: Beaven, G D.E.]] |
| - | [[Category: Brindley, A | + | [[Category: Brindley, A A.]] |
[[Category: Coates, L.]] | [[Category: Coates, L.]] | ||
| - | [[Category: Cooper, J | + | [[Category: Cooper, J B.]] |
| - | [[Category: Erskine, P | + | [[Category: Erskine, P T.]] |
[[Category: Gill, R.]] | [[Category: Gill, R.]] | ||
[[Category: Neier, R.]] | [[Category: Neier, R.]] | ||
[[Category: Newbold, R.]] | [[Category: Newbold, R.]] | ||
| - | [[Category: Shoolingin-Jordan, P | + | [[Category: Shoolingin-Jordan, P M.]] |
[[Category: Stauffer, F.]] | [[Category: Stauffer, F.]] | ||
| - | [[Category: Warren, M | + | [[Category: Warren, M J.]] |
| - | [[Category: Wood, S | + | [[Category: Wood, S P.]] |
[[Category: SHO]] | [[Category: SHO]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
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[[Category: zinc]] | [[Category: zinc]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:39:55 2008'' |
Revision as of 13:39, 21 February 2008
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YEAST 5-AMINOLAEVULINIC ACID DEHYDRATASE 5-HYDROXYLAEVULINIC ACID COMPLEX
Overview
The X-ray structure of the enzyme 5-aminolaevulinic acid dehydratase (ALAD) from yeast complexed with the competitive inhibitor 5-hydroxylaevulinic acid has been determined at a resolution of 1.9 A. The structure shows that the inhibitor is bound by a Schiff-base link to one of the invariant active-site lysine residues (Lys263). The inhibitor appears to bind in two well defined conformations and the interactions made by it suggest that it is a very close analogue of the substrate 5-aminolaevulinic acid (ALA).
About this Structure
1W31 is a Single protein structure of sequence from Saccharomyces cerevisiae with and as ligands. Active as Porphobilinogen synthase, with EC number 4.2.1.24 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Structure of yeast 5-aminolaevulinic acid dehydratase complexed with the inhibitor 5-hydroxylaevulinic acid., Erskine PT, Coates L, Newbold R, Brindley AA, Stauffer F, Beaven GD, Gill R, Coker A, Wood SP, Warren MJ, Shoolingin-Jordan PM, Neier R, Cooper JB, Acta Crystallogr D Biol Crystallogr. 2005 Sep;61(Pt 9):1222-6. Epub 2005, Aug 16. PMID:16131755
Page seeded by OCA on Thu Feb 21 15:39:55 2008
Categories: Porphobilinogen synthase | Saccharomyces cerevisiae | Single protein | Beaven, G D.E. | Brindley, A A. | Coates, L. | Cooper, J B. | Erskine, P T. | Gill, R. | Neier, R. | Newbold, R. | Shoolingin-Jordan, P M. | Stauffer, F. | Warren, M J. | Wood, S P. | SHO | ZN | Aldolase | Dehydratase | Heme biosynthesis | Lyase | Tetrapyrrole synthesis | Tim barrel | Zinc
