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Published online before print September 30, 2004, 10.1110/ps.041012404
Protein Science (2004), 13:3038-3042. Published by Cold Spring Harbor Laboratory Press. Copyright © 2004 The Protein Society
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PROTEIN STRUCTURE REPORT

Crystal structures of possible lysine decarboxylases from Thermus thermophilus HB8

Mutsuko Kukimoto-Niino1, Kazutaka Murayama1, Miyuki Kato-Murayama1, Miki Idaka1, Yoshitaka Bessho1, Ayako Tatsuguchi1, Ryoko Ushikoshi-Nakayama1, Takaho Terada1,2, Seiki Kuramitsu2,3, Mikako Shirouzu1,2 and Shigeyuki Yokoyama1,2,4

1 RIKEN Genomic Sciences Center, Tsurumi, Yokohama 230-0045, Japan
2 RIKEN Harima Institute at SPring-8, Mikazuki-cho, Sayo, Hyogo 679-5148, Japan
3 Graduate School of Science, Osaka University, Toyonaka, Osaka 560–0043, Japan
4 Graduate School of Science, The University of Tokyo, Bunkyo-ku, Tokyo 113-0033, Japan

(RECEIVED August 3, 2004; FINAL REVISION August 3, 2004; ACCEPTED August 6, 2004)

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. TT1887 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 {alpha} helices and seven {beta} strands, and are quite similar to each other. The major structural differences exist in the N terminus of TT1465, where there are two additional {alpha} 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.

Keywords: structural genomics; Thermus thermophilus; hypothetical protein; lysine decarboxylase; Rossmann fold

Reprint requests to: Shigeyuki Yokoyama, RIKEN Genomic Sciences Center, 1–7–22 Suehirocho, Tsurumi, Yokohama 230-0045, Japan; e-mail: yokoyama{at}biochem.s.u-tokyo.ac.jp; fax: +81-45-503-9195.


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