2qlx
From Proteopedia
Crystal structure of rhamnose mutarotase RhaU of Rhizobium leguminosarum in complex with L-Rhamnose
Structural highlights
FunctionRHAM_RHILT Involved in the anomeric conversion of L-rhamnose.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedOf the nine genes comprising the L-rhamnose operon of Rhizobium leguminosarum, rhaU has not been assigned a function. The construction of a Delta rhaU strain revealed a growth phenotype that was slower than that of the wild-type strain, although the ultimate cell yields were equivalent. The transport of L-rhamnose into the cell and the rate of its phosphorylation were unaffected by the mutation. RhaU exhibits weak sequence similarity to the formerly hypothetical protein YiiL of Escherichia coli that has recently been characterized as an L-rhamnose mutarotase. To characterize RhaU further, a His-tagged variant of the protein was prepared and subjected to mass spectrometry analysis, confirming the subunit size and demonstrating its dimeric structure. After crystallization, the structure was refined to a 1.6-A resolution to reveal a dimer in the asymmetric unit with a very similar structure to that of YiiL. Soaking a RhaU crystal with L-rhamnose resulted in the appearance of beta-L-rhamnose in the active site. RhaU of Rhizobium leguminosarum is a rhamnose mutarotase.,Richardson JS, Carpena X, Switala J, Perez-Luque R, Donald LJ, Loewen PC, Oresnik IJ J Bacteriol. 2008 Apr;190(8):2903-10. Epub 2007 Dec 21. PMID:18156270[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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