1MGP

Hypothetical protein TM841 from Thermotoga maritima reveals fatty acid binding function

Summary for 1MGP

• Entry DOI: 10.2210/pdb1mgp/pdb
• Descriptor: Hypothetical protein TM841, PALMITIC ACID (3 entities in total)
• Functional Keywords: two domain structure with mixed alpha/beta structures in both domains, structural genomics, bsgc structure funded by nih, protein structure initiative, psi, berkeley structural genomics center, lipid binding protein
• Biological source: Thermotoga maritima
• Total number of polymer chains: 1
• Total formula weight: 36193.43

Authors

Schulze-Gahmen, U.,Pelaschier, J.,Yokota, H.,Kim, R.,Kim, S.-H.,Berkeley Structural Genomics Center (BSGC) (deposition date: 2002-08-15, release date: 2002-09-18, Last modification date: 2024-10-16)

Primary citation

Schulze-Gahmen, U.,Pelaschier, J.,Yokota, H.,Kim, R.,Kim, S.-H.
Crystal structure of a hypothetical protein, TM841 of Thermotoga maritima, reveals its function as fatty acid binding protein
Proteins, 50:526-530, 2003

PubMed Abstract: 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 A 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.

PubMed: 12577257
DOI: 10.1002/prot.10305

Experimental method

X-RAY DIFFRACTION (2 Å)