Crystal structure of a hypothetical protein, TM841 of Thermotoga maritima, reveals its function as a fatty acid-binding protein

被引：35

作者：

Schulze-Gahmen, U

Pelaschier, J

Yokota, H

Kim, R

Kim, SH

机构：

[1] Univ Calif Berkeley, Dept Chem, Berkeley, CA 94720 USA

[2] Univ Calif Berkeley, Lawrence Berkeley Lab, Phys Biosci Div, Berkeley, CA USA

来源：

PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS | 2003年 / 50卷 / 04期

关键词：

X-ray crystallography; structural genomics; lipid-binding protein; DegV protein family; LIPID-TRANSFER PROTEIN; DATABASE; STATE;

D O I：

10.1002/prot.10305

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 Angstrom 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. (C) 2003 Wiley-Liss, Inc.

引用

页码：526 / 530

页数：5

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