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Tsai, T.-Y., Yang, C.-Y., Shih, H.-L., Wang, A.H.J. and Chou, S.-H. (2009) Xanthomonas campestris PqqD in the pyrroloquinoline quinone biosynthesis operon adopts a novel saddle-like fold that possibly serves as a PQQ carrier. Proteins: Structure, Function, and Bioinformatics, 76, 1042-1048. doi:10.1002/prot.22461

has been cited by the following article:

• TITLE: Crystal structure of PqqB from Pseudomonas putida at 2.2 Å resolution

  AUTHORS: Moritz Metlitzky, Sandra Puehringer, Stuart J. Fisher

  KEYWORDS: PqqB; PQQ; Biosynthetic Pathway; X-Ray Crystallography

  JOURNAL NAME: Journal of Biophysical Chemistry, Vol.3 No.2, May 29, 2012

  ABSTRACT: Pyrroloquinoline quinone (PQQ) is an important redox-active cofactor for many bacterial dehy-drogenases. It's biosynthetic pathway involves six or seven genes, one of which is pqqB. Former studies indicated that the protein encoded by pqqB, namely PqqB, functions as a PQQ transporter. Here we report the crystal structure of PqqB from Pseudomonas putida at 2.2 ? resolution together with functional studies to verify this theory.