X-ray crystal structure of Saccharomyces cerevisiae Pdx1 provides insights into the oligomeric nature of PLP synthases
X-ray crystal structure of Saccharomyces cerevisiae Pdx1 provides insights into the oligomeric nature of PLP synthases
The universal enzymatic cofactor vitamin B6 can be synthesized as pyridoxal 5-phosphate (PLP) by the glutamine amidotransferase Pdx1. We show that Saccharomyces cerevisiae Pdx1 is hexameric by analytical ultracentrifugation and by crystallographic 3D structure determination. Bacterial homologues were previously reported to exist in hexamer:dodecamer equilibrium. A small sequence insertion found in yeast Pdx1 elevates the dodecamer dissociation constant when introduced into Bacillus subtilis Pdx1. Further, we demonstrate that the yeast Pdx1 C-terminus contacts an adjacent subunit, and deletion of this segment decreases enzymatic activity 3.5-fold, suggesting a role in catalysis.
glutamine amidotransferase, vitamin b6 (pyridoxal 5-phosphate), pdx, snz, oligomerisation, x-ray structure, twinning
2179-2186
Neuwirth, Martina
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Strohmeier, Marco
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Windeisen, Volker
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Wallner, Silvia
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Deller, Sigrid
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Rippe, Karsten
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Sinning, Irmgard
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Macheroux, Peter
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Tews, Ivo
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7 July 2009
Neuwirth, Martina
6ea2236b-a98c-48b3-a908-52fb9b318ff8
Strohmeier, Marco
945de88c-2eb8-4708-b91b-8f599b4b8c24
Windeisen, Volker
904d85ea-64f9-4157-b273-031e5dbc0f76
Wallner, Silvia
147f37c7-9e66-40f5-9296-89e910237ad6
Deller, Sigrid
7c500fe3-830e-4ace-898e-04fb95801247
Rippe, Karsten
5dc8f1ed-943d-42d2-baa6-1e7f777f391e
Sinning, Irmgard
fbc3f199-8a3b-47a6-9ee7-00bfc472e079
Macheroux, Peter
e1c49266-c971-42f7-86ae-394bd128d040
Tews, Ivo
9117fc5e-d01c-4f8d-a734-5b14d3eee8dd
Neuwirth, Martina, Strohmeier, Marco, Windeisen, Volker, Wallner, Silvia, Deller, Sigrid, Rippe, Karsten, Sinning, Irmgard, Macheroux, Peter and Tews, Ivo
(2009)
X-ray crystal structure of Saccharomyces cerevisiae Pdx1 provides insights into the oligomeric nature of PLP synthases.
FEBS Letters, 583 (13), .
(doi:10.1016/j.febslet.2009.06.009).
(PMID:19523954)
Abstract
The universal enzymatic cofactor vitamin B6 can be synthesized as pyridoxal 5-phosphate (PLP) by the glutamine amidotransferase Pdx1. We show that Saccharomyces cerevisiae Pdx1 is hexameric by analytical ultracentrifugation and by crystallographic 3D structure determination. Bacterial homologues were previously reported to exist in hexamer:dodecamer equilibrium. A small sequence insertion found in yeast Pdx1 elevates the dodecamer dissociation constant when introduced into Bacillus subtilis Pdx1. Further, we demonstrate that the yeast Pdx1 C-terminus contacts an adjacent subunit, and deletion of this segment decreases enzymatic activity 3.5-fold, suggesting a role in catalysis.
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e-pub ahead of print date: 11 June 2009
Published date: 7 July 2009
Additional Information:
Funded by European Commission - FP6: Vitamin biosynthesis as a target for antimalarial therapy (VITBIOMAL) (12158)
Keywords:
glutamine amidotransferase, vitamin b6 (pyridoxal 5-phosphate), pdx, snz, oligomerisation, x-ray structure, twinning
Organisations:
Centre for Biological Sciences
Identifiers
Local EPrints ID: 200335
URI: http://eprints.soton.ac.uk/id/eprint/200335
ISSN: 0014-5793
PURE UUID: fac055de-4da3-42ef-a83e-bf509b842bae
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Date deposited: 26 Oct 2011 11:17
Last modified: 15 Mar 2024 03:36
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Contributors
Author:
Martina Neuwirth
Author:
Marco Strohmeier
Author:
Volker Windeisen
Author:
Silvia Wallner
Author:
Sigrid Deller
Author:
Karsten Rippe
Author:
Irmgard Sinning
Author:
Peter Macheroux
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