Structure of yeast 5-aminolaevulinic acid dehydratase complexed with the inhibitor 5-hydroxylaevulinic acid

P. T. Erskine; L. Coates; R. Newbold; A. A. Brindley; F. Stauffer; G. D. E. Beaven; R. Gill; A. Coker; S. P. Wood; M. J. Warren; P. M. Shoolingin-Jordan; R. Neier; J. B. Cooper

doi:10.1107/S0907444905018834

Structure of yeast 5-aminolaevulinic acid dehydratase complexed with the inhibitor 5-hydroxylaevulinic acid

P. T. Erskine
, L. Coates
, R. Newbold
, A. A. Brindley
, F. Stauffer
, G. D. E. Beaven
, R. Gill
, A. Coker
, S. P. Wood
, M. J. Warren
, P. M. Shoolingin-Jordan
, R. Neier
, J. B. Cooper

Research output: Contribution to journal › Article › peer-review

Abstract

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).

Original language	English
Pages (from-to)	1222-6
Number of pages	5
Journal	Acta Crystallographica Section D
Volume	D61
Issue number	Pt 9
DOIs	https://doi.org/10.1107/S0907444905018834
Publication status	Published - Sept 2005

Keywords

Aminolevulinic Acid/analogs & derivatives
Binding Sites
Crystallography, X-Ray
Fungal Proteins/chemistry
Molecular Structure
Porphobilinogen Synthase/antagonists & inhibitors
Protein Conformation
Schiff Bases

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10.1107/S0907444905018834

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Erskine, P. T., Coates, L., Newbold, R., Brindley, A. A., Stauffer, F., Beaven, G. D. E., Gill, R., Coker, A., Wood, S. P., Warren, M. J., Shoolingin-Jordan, P. M., Neier, R., & Cooper, J. B. (2005). Structure of yeast 5-aminolaevulinic acid dehydratase complexed with the inhibitor 5-hydroxylaevulinic acid. Acta Crystallographica Section D, D61(Pt 9), 1222-6. https://doi.org/10.1107/S0907444905018834

@article{f82f2635bdff4b93aa4993db2b275e97,

title = "Structure of yeast 5-aminolaevulinic acid dehydratase complexed with the inhibitor 5-hydroxylaevulinic acid",

abstract = "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).",

keywords = "Aminolevulinic Acid/analogs \& derivatives, Binding Sites, Crystallography, X-Ray, Fungal Proteins/chemistry, Molecular Structure, Porphobilinogen Synthase/antagonists \& inhibitors, Protein Conformation, Schiff Bases",

author = "Erskine, \{P. T.\} and L. Coates and R. Newbold and Brindley, \{A. A.\} and F. Stauffer and Beaven, \{G. D. E.\} and R. Gill and A. Coker and Wood, \{S. P.\} and Warren, \{M. J.\} and Shoolingin-Jordan, \{P. M.\} and R. Neier and Cooper, \{J. B.\}",

year = "2005",

month = sep,

doi = "10.1107/S0907444905018834",

language = "English",

volume = "D61",

pages = "1222--6",

journal = "Acta Crystallographica Section D",

issn = "0907-4449",

publisher = "International Union of Crystallography",

number = "Pt 9",

}

Erskine, PT, Coates, L, Newbold, R, Brindley, AA, Stauffer, F, Beaven, GDE, Gill, R, Coker, A, Wood, SP, Warren, MJ, Shoolingin-Jordan, PM, Neier, R & Cooper, JB 2005, 'Structure of yeast 5-aminolaevulinic acid dehydratase complexed with the inhibitor 5-hydroxylaevulinic acid', Acta Crystallographica Section D, vol. D61, no. Pt 9, pp. 1222-6. https://doi.org/10.1107/S0907444905018834

TY - JOUR

T1 - Structure of yeast 5-aminolaevulinic acid dehydratase complexed with the inhibitor 5-hydroxylaevulinic acid

AU - Erskine, P. T.

AU - Coates, L.

AU - Newbold, R.

AU - Brindley, A. A.

AU - Stauffer, F.

AU - Beaven, G. D. E.

AU - Gill, R.

AU - Coker, A.

AU - Wood, S. P.

AU - Warren, M. J.

AU - Shoolingin-Jordan, P. M.

AU - Neier, R.

AU - Cooper, J. B.

PY - 2005/9

Y1 - 2005/9

N2 - 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).

AB - 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).

KW - Aminolevulinic Acid/analogs & derivatives

KW - Binding Sites

KW - Crystallography, X-Ray

KW - Fungal Proteins/chemistry

KW - Molecular Structure

KW - Porphobilinogen Synthase/antagonists & inhibitors

KW - Protein Conformation

KW - Schiff Bases

U2 - 10.1107/S0907444905018834

DO - 10.1107/S0907444905018834

M3 - Article

C2 - 16131755

SN - 0907-4449

VL - D61

SP - 1222

EP - 1226

JO - Acta Crystallographica Section D

JF - Acta Crystallographica Section D

IS - Pt 9

ER -

Structure of yeast 5-aminolaevulinic acid dehydratase complexed with the inhibitor 5-hydroxylaevulinic acid

Abstract

Keywords

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