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Journal of Bacteriology, June 2007, p. 4520-4528, Vol. 189, No. 12
0021-9193/07/$08.00+0 doi:10.1128/JB.00277-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.
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Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Apartado 127, 2781-901 Oeiras, Portugal,1 European Synchrotron Radiation Facility, Bp-220, F-38043 Grenoble Cedex, France,2 Institute for Biotechnology and Bioengineering, Center for Biological and Chemical Engineering, Instituto Superior Técnico, 1049-001 Lisbon, Portugal3
Received 19 February 2007/ Accepted 2 March 2007
Gellan gum is a widely used commercial material, available in many different forms. Its economic importance has led to studies into the biosynthesis of exopolysaccharide gellan gum, which is industrially prepared in high yields using Sphingomonas elodea ATCC 31461. Glucose-1-phosphate uridylyltransferase mediates the reversible conversion of glucose-1-phosphate and UTP into UDP-glucose and pyrophosphate, which is a key step in the biosynthetic pathway of gellan gums. Here we present the X-ray crystal structure of the glucose-1-phosphate uridylyltransferase from S. elodea. The S. elodea enzyme shares strong monomeric similarity with glucose-1-phosphate thymidylyltransferase, several structures of which are known, although the quaternary structures of the active enzymes are rather different. A detailed comparison between S. elodea glucose-1-phosphate uridylyltransferase and available thymidylyltransferases is described and shows remarkable structural similarities, despite the low sequence identities between the two divergent groups of proteins.
Published ahead of print on 13 April 2007.
Supplemental material for this article may be found at http://jb.asm.org/.
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