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

5 Scopus citations

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 Å. 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)	1222-1226
Number of pages	5
Journal	Acta Crystallographica Section D: Biological Crystallography
Volume	61
Issue number	9
DOIs	https://doi.org/10.1107/S0907444905018834
State	Published - Sep 2005
Externally published	Yes

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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: Biological Crystallography, 61(9), 1222-1226. https://doi.org/10.1107/S0907444905018834

@article{7040d075853e4b25891d3b7cd48d124c,

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 {\AA}. 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).",

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 = "61",

pages = "1222--1226",

journal = "Acta Crystallographica Section D: Biological Crystallography",

issn = "0907-4449",

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}

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: Biological Crystallography, vol. 61, no. 9, pp. 1222-1226. 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 Å. 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 Å. 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).

UR - https://www.scopus.com/pages/publications/32944481924

U2 - 10.1107/S0907444905018834

DO - 10.1107/S0907444905018834

M3 - Article

C2 - 16131755

AN - SCOPUS:32944481924

SN - 0907-4449

VL - 61

SP - 1222

EP - 1226

JO - Acta Crystallographica Section D: Biological Crystallography

JF - Acta Crystallographica Section D: Biological Crystallography

IS - 9

ER -

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

Abstract

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