The University of Southampton
University of Southampton Institutional Repository

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

Structure of yeast 5-aminolaevulinic acid dehydratase complexed with the inhibitor 5-hydroxylaevulinic acid
Structure of yeast 5-aminolaevulinic acid dehydratase complexed with the inhibitor 5-hydroxylaevulinic acid
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).
5-aminolaevulinic acid dehydratase, 1w31, r1w31sf.
0907-4449
1222-1226
Erskine, P.T.
c77b60c5-b80c-4e6a-a103-bf57ecfcbcf6
Coates, L.
2be36c11-8cb2-4518-a001-953051aa6a23
Newbold, R.
fa67a143-11e2-4e5d-8870-56db80d2f713
Brindley, A.A.
638ed87e-b0f7-4e74-9433-13bcde83aafc
Stauffer, F.
69658c3a-ac98-4259-994e-efab08e13fcd
Beaven, G.D.E
bfba062d-06fd-4c94-821c-23cfdf438304
Gill, R.
95656ecb-604f-425e-ac66-7dd36e47d94d
Coker, A.
c64a7d9b-3a0d-4e79-a3eb-aaa64920116a
Wood, S.P.
430faabf-7f5c-4cf6-9bcc-5955f5e09566
Warren, M.J.
6dc30bb6-c290-490e-8aab-44ad27c7c609
Shoolingin-Jordan, P.M.
ac0bf2cc-ee36-4b30-bcef-525cee2559f7
Neier, R.
8dbdc1db-e80b-4f92-a608-dd97577793d6
Cooper, J.B.
d9f0f6a8-1260-48fc-aa5c-3dbc650e3ec0
Erskine, P.T.
c77b60c5-b80c-4e6a-a103-bf57ecfcbcf6
Coates, L.
2be36c11-8cb2-4518-a001-953051aa6a23
Newbold, R.
fa67a143-11e2-4e5d-8870-56db80d2f713
Brindley, A.A.
638ed87e-b0f7-4e74-9433-13bcde83aafc
Stauffer, F.
69658c3a-ac98-4259-994e-efab08e13fcd
Beaven, G.D.E
bfba062d-06fd-4c94-821c-23cfdf438304
Gill, R.
95656ecb-604f-425e-ac66-7dd36e47d94d
Coker, A.
c64a7d9b-3a0d-4e79-a3eb-aaa64920116a
Wood, S.P.
430faabf-7f5c-4cf6-9bcc-5955f5e09566
Warren, M.J.
6dc30bb6-c290-490e-8aab-44ad27c7c609
Shoolingin-Jordan, P.M.
ac0bf2cc-ee36-4b30-bcef-525cee2559f7
Neier, R.
8dbdc1db-e80b-4f92-a608-dd97577793d6
Cooper, J.B.
d9f0f6a8-1260-48fc-aa5c-3dbc650e3ec0

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. and 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, 1222-1226. (doi:10.1107/S0907444905018834).

Record type: Article

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).

PDF
Coker2_05.pdf - Other
Restricted to Registered users only
Download (1MB)
Request a copy

More information

Submitted date: 21 July 2004
Published date: 2005
Keywords: 5-aminolaevulinic acid dehydratase, 1w31, r1w31sf.

Identifiers

Local EPrints ID: 24094
URI: https://eprints.soton.ac.uk/id/eprint/24094
ISSN: 0907-4449
PURE UUID: 72afa51e-3314-46a3-a849-6eb80f9cc4e4

Catalogue record

Date deposited: 22 Mar 2006
Last modified: 17 Jul 2017 16:15

Export record

Altmetrics

Contributors

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

University divisions

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton: eprints@soton.ac.uk

ePrints Soton supports OAI 2.0 with a base URL of https://eprints.soton.ac.uk/cgi/oai2

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.

×