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Backbone 1H, 13C, 15N NMR assignments of yeast OMP synthase in unliganded form and in complex with orotidine 5′-monophosphate

Backbone 1H, 13C, 15N NMR assignments of yeast OMP synthase in unliganded form and in complex... The type I phosphoribosyltransferase OMP synthase (EC 2.4.2.10) is involved in de novo synthesis of pyrimidine nucleotides forming the UMP precursor orotidine 5′-monophosphate (OMP). The homodimeric enzyme has a Rossman α/β core topped by a base-enclosing “hood” domain and a flexible domain-swapped catalytic loop. High-resolution X-ray structures of the homologous Salmonella typhimurium and yeast enzymes show that a general compacting of the core as well as movement of the hood and a major disorder-to-order transition of the loop occur upon binding of ligands MgPRPP and orotate. Here we present backbone NMR assignments for the unliganded yeast enzyme (49 kDa) and its complex with product OMP. We were able to assign 212–213 of the 225 non-proline backbone 15N and amide proton resonances. Significant difference in chemical shifts of the amide cross peaks occur in regions of the structure that undergo movement upon ligand occupancy in the S. typhimurium enzyme. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biomolecular NMR Assignments Springer Journals

Backbone 1H, 13C, 15N NMR assignments of yeast OMP synthase in unliganded form and in complex with orotidine 5′-monophosphate

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Publisher
Springer Journals
Copyright
Copyright © 2013 by Springer Science+Business Media Dordrecht
Subject
Physics; Biophysics and Biological Physics; Polymer Sciences; Biochemistry, general
ISSN
1874-2718
eISSN
1874-270X
DOI
10.1007/s12104-013-9462-x
pmid
23315339
Publisher site
See Article on Publisher Site

Abstract

The type I phosphoribosyltransferase OMP synthase (EC 2.4.2.10) is involved in de novo synthesis of pyrimidine nucleotides forming the UMP precursor orotidine 5′-monophosphate (OMP). The homodimeric enzyme has a Rossman α/β core topped by a base-enclosing “hood” domain and a flexible domain-swapped catalytic loop. High-resolution X-ray structures of the homologous Salmonella typhimurium and yeast enzymes show that a general compacting of the core as well as movement of the hood and a major disorder-to-order transition of the loop occur upon binding of ligands MgPRPP and orotate. Here we present backbone NMR assignments for the unliganded yeast enzyme (49 kDa) and its complex with product OMP. We were able to assign 212–213 of the 225 non-proline backbone 15N and amide proton resonances. Significant difference in chemical shifts of the amide cross peaks occur in regions of the structure that undergo movement upon ligand occupancy in the S. typhimurium enzyme.

Journal

Biomolecular NMR AssignmentsSpringer Journals

Published: Jan 12, 2013

References