Crystal structures of possible lysine decarboxylases from Thermus thermophilus HB8

Mutsuko Kukimoto-Niino, Kazutaka Murayama, Miyuki Kato-Murayama, Miki Idaka, Yoshitaka Bessho, Ayako Tatsuguchi, Ryoko Ushikoshi-Nakayama, Takaho Terada, Seiki Kuramitsu, Mikako Shirouzu, Shigeyuki Yokoyama

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10 Citations (Scopus)


TT1887 and TT1465 from Thermus thermophilus HB8 are conserved hypothetical proteins, and are annotated as possible lysine decarboxylases in the Pfam database. Here we report the crystal structures of TT1887 and TT1465 at 1.8 Å and 2.2 Å resolutions, respectively, as determined by the multiwavelength anomalous dispersion (MAD) method. TT1387 is a homotetramer, while TT1465 is a homohexamer in the crystal and in solution. The structures of the TT1887 and TT1465 monomers contain single domains with the Rossmann fold, comprising six α helices and seven β strands, and are quite similar to each other. The major structural differences exist in the N terminus of TT1465, where there are two additional α helices. A comparison of the structures revealed the elements that are responsible for the different oligomerization modes. The distributions of the electrostatic potential on the solvent-accessible surfaces suggested putative active sites.

Original languageEnglish
Pages (from-to)3038-3042
Number of pages5
JournalProtein Science
Issue number11
Publication statusPublished - 2004 Nov


  • Hypothetical protein
  • Lysine decarboxylase
  • Rossmann fold
  • Structural genomics
  • Thermus thermophilus


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