1S12
Crystal structure of TM1457
Summary for 1S12
Entry DOI | 10.2210/pdb1s12/pdb |
Descriptor | hypothetical protein TM1457, ACETATE ION (3 entities in total) |
Functional Keywords | crystal, structural genomics, hypothetical protein, psi, berkeley structural genomics center, bsgc, protein structure initiative, unknown function |
Biological source | Thermotoga maritima |
Total number of polymer chains | 4 |
Total formula weight | 42465.56 |
Authors | Shin, D.H.,Lou, Y.,Jancarik, J.,Yokota, H.,Kim, R.,Kim, S.-H.,Berkeley Structural Genomics Center (BSGC) (deposition date: 2004-01-05, release date: 2004-12-07, Last modification date: 2024-10-30) |
Primary citation | Shin, D.H.,Lou, Y.,Jancarik, J.,Yokota, H.,Kim, R.,Kim, S.H. Crystal structure of TM1457 from Thermotoga maritima. J.Struct.Biol., 152:113-117, 2005 Cited by PubMed Abstract: The crystal structure of a hypothetical protein, TM1457, from Thermotoga maritima has been determined at 2.0A 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 beta-sheet. Two identical monomers form a pseudo-dimer in the asymmetric unit. There is a large cleft between the first alpha-helix and the second beta-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. PubMed: 16242963DOI: 10.1016/j.jsb.2005.08.008 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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