1mgp
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(New page: 200px<br /><applet load="1mgp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mgp, resolution 2.00Å" /> '''Hypothetical protein...)
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Revision as of 19:17, 20 November 2007
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Hypothetical protein TM841 from Thermotoga maritima reveals fatty acid binding function
Overview
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.
About this Structure
1MGP is a Single protein structure of sequence from Thermotoga maritima with PLM as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of a hypothetical protein, TM841 of Thermotoga maritima, reveals its function as a fatty acid-binding protein., Schulze-Gahmen U, Pelaschier J, Yokota H, Kim R, Kim SH, Proteins. 2003 Mar 1;50(4):526-30. PMID:12577257
Page seeded by OCA on Tue Nov 20 21:24:16 2007
Categories: Single protein | Thermotoga maritima | BSGC, Berkeley.Structural.Genomics.Center. | Kim, R. | Kim, S.H. | Pelaschier, J. | Schulze-Gahmen, U. | Yokota, H. | PLM | Berkeley structural genomics center | Bsgc structure funded by nih | Protein structure initiative | Psi | Structural genomics | Two domain structure with mixed alpha/beta structures in both domains