Premium
Crystal structure of a hypothetical protein, TM841 of Thermotoga maritima , reveals its function as a fatty acid–binding protein
Author(s) -
SchulzeGahmen Ursula,
Pelaschier Joanne,
Yokota Hisao,
Kim Rosalind,
Kim SungHou
Publication year - 2003
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.10305
Subject(s) - thermotoga maritima , hyperthermophile , biochemistry , protein structure , function (biology) , structural genomics , fatty acid , chemistry , biology , crystallography , gene , archaea , microbiology and biotechnology , escherichia coli
We determined the three‐dimensional (3D) crystal structure of protein TM841, a protein product from a hypothetical open‐reading frame in the genome of the hyperthermophile bacterium Thermotoga maritima, to 2.0 Å resolution. The protein belongs to a large protein family, DegV or COG1307 of unknown function. The 35 kDa protein consists of two separate domains, with low‐level structural resemblance to domains from other proteins with known 3D structures. These structural homologies, however, provided no clues for the function of TM841. But the electron density maps revealed clear density for a bound fatty‐acid molecule in a pocket between the two protein domains. The structure indicates that TM841 has the molecular function of fatty‐acid binding and may play a role in the cellular functions of fatty acid transport or metabolism. Proteins 2003;50:526–530. © 2003 Wiley‐Liss, Inc.