2D4R
Crystal structure of TTHA0849 from Thermus thermophilus HB8
Summary for 2D4R
Entry DOI | 10.2210/pdb2d4r/pdb |
Descriptor | hypothetical protein TTHA0849, SULFATE ION (3 entities in total) |
Functional Keywords | start domain, structural genomics, riken structural genomics/proteomics initiative, rsgi, unknown function |
Biological source | Thermus thermophilus |
Total number of polymer chains | 4 |
Total formula weight | 69089.10 |
Authors | Nakabayashi, M.,Shibata, N.,Kuramitsu, S.,Higuchi, Y.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2005-10-23, release date: 2005-12-13, Last modification date: 2024-10-23) |
Primary citation | Nakabayashi, M.,Shibata, N.,Komori, H.,Ueda, Y.,Iino, H.,Ebihara, A.,Kuramitsu, S.,Higuchi, Y. Structure of a conserved hypothetical protein, TTHA0849 from Thermus thermophilus HB8, at 2.4 A resolution: a putative member of the StAR-related lipid-transfer (START) domain superfamily. Acta Crystallogr.,Sect.F, 61:1027-1031, 2005 Cited by PubMed Abstract: The crystal structure of a conserved hypothetical protein, TTHA0849 from Thermus thermophilus HB8, has been determined at 2.4 A resolution as a part of a structural and functional genomics project on T. thermophilus HB8. The main-chain folding shows a compact alpha+beta motif, forming a hydrophobic cavity in the molecule. A structural similarity search reveals that it resembles those steroidogenic acute regulatory proteins that contain the lipid-transfer (START) domain, even though TTHA0849 shows comparatively weak sequence identity to polyketide cyclases. However, the size of the ligand-binding cavity is distinctly smaller than other START domain-containing proteins, suggesting that it catalyses the transfer of smaller ligand molecules. PubMed: 16511226DOI: 10.1107/S1744309105035372 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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