RhaU of Rhizobium leguminosarum is a rhamnose mutarotase.

Abstract:

:Of 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.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Richardson JS,Carpena X,Switala J,Perez-Luque R,Donald LJ,Loewen PC,Oresnik IJ

doi

10.1128/JB.01120-07

subject

Has Abstract

pub_date

2008-04-01 00:00:00

pages

2903-10

issue

8

eissn

0021-9193

issn

1098-5530

pii

JB.01120-07

journal_volume

190

pub_type

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