Structural characterization of Helicobacter pylori dethiobiotin synthetase reveals differences between family members (pages 1093–1105)
Przemyslaw J. Porebski, Maria Klimecka, Maksymilian Chruszcz, Robert A. Nicholls, Krzysztof Murzyn, Marianne E. Cuff, Xiaohui Xu, Marcin Cymborowski, Garib N. Murshudov, Alexei Savchenko, Aled Edwards and Wladek Minor
Article first published online: 27 FEB 2012 | DOI: 10.1111/j.1742-4658.2012.08506.x
We determined structures of DBTS from H. pylori (hpDTBS) bound with cofactors and a substrate analog. We have shown that the C-terminal region of DTBSes, which contains two nucleotide-recognition motifs, greatly differs among DTBSes. hpDTBS is characterized by a unique mode of nucleotide recognition–it does not contain a C-terminal region containing one of the motifs, but it is ATP specific.