doi:10.1016/j.jsb.2005.08.008 
Copyright © 2005 Elsevier Inc. All rights reserved.
Crystal structure of TM1457 from Thermotoga maritima
Dong Hae Shina, b, Yun Loub, Jaru Jancarikb, Hisao Yokotab, Rosalind Kimb and Sung-Hou Kimb, c, 
, 
aCollege of Pharmacy, Ewha Womans University, Seoul 120-750, Korea
bBerkeley Structural Genomics Center, Physical Bioscience Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA
cDepartment of Chemistry, University of California, Berkeley, CA 94720-5230, USA
Received 12 April 2005;
revised 19 August 2005;
accepted 23 August 2005.
Available online 3 October 2005.
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Abstract
The crystal structure of a hypothetical protein, TM1457, from Thermotoga maritima has been determined at 2.0 Å resolution. TM1457 belongs to the DUF464 family (57 members) for which there is no known function. The structure shows that it is composed of two helices in contact with one side of a five-stranded β-sheet. Two identical monomers form a pseudo-dimer in the asymmetric unit. There is a large cleft between the first α-helix and the second β-strand. This cleft may be functionally important, since the two highly conserved motifs, GHA and VCAXV(S/T), are located around the cleft. A structural comparison of TM1457 with known protein structures shows the best hit with another hypothetical protein, Ybl001C from Saccharomyces cerevisiae, though they share low structural similarity. Therefore, TM1457 still retains a unique topology and reveals a novel fold.
Keywords: TM1457; Gi 4982022; Crystal structure; Hypothetical protein; DUF464
Fig. 1. Sequence comparison among some members of DUF464 family. Abbreviations are as follows: DUF464 from Streptococcus pyogenes M1 GAS (SpDUF464); DUF464 from S. pneumoniae TIGR4 (SpDUF464), DUF464 from Bacillus subtilis (BsDUF464); DUF464 from Lactococcus lactis subsp. Lactis (LlDUF464); DUF464 from Ureaplasma urealyticum (UuDUF464); MPN326 from M. pneumoniae. The “-”s represent gaps, “*” for identical residues, “:” for homologous residues, and “.” for semi-homologue residues (www.ebi.ac.uk/clustalw).
Fig. 2. (A) A stereo drawing of a Cα trace of TM1475. The model is represented by a thick line with rainbow colors. Every 20th residue is numbered and represented by a dot. The N (residue Met1) and C-termini (residue Ser94) are labeled. The figure was generated by MOLSCRIPT (Kraulis, 1991). (B) Two views of TM1475 in an asymmetric unit. Two views are presented: one subunit with a yellow wireworm model and the other as an electrostatic surface potential drawn with the program GRASP (red, negative; blue, positive; white, uncharged) (Nicholls, 1991). The highly conserved residues are labeled on the molecular surface. Two bound acetates are represented with a ball-and-stick model. Arg72 is labeled on the molecular surface.
Fig. 3. A stereo drawing of superposition of TM1475 with several homologues. The stereo drawing is represented in blue for TM1475, in red for Ybl001C from Saccharomyces cerevisiae, in yellow for urocanate hydratase from Pseudomonas putida (residues from 437 to 537), and in green for chemotaxis protein CheA from T. maritima (residues from 301 to 356).
Table 1B.
Crystal parameters and refinement statistics
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