2EF7
Crystal structure of ST2348, a hypothetical protein with CBS domains from Sulfolobus tokodaii strain7
Summary for 2EF7
| Entry DOI | 10.2210/pdb2ef7/pdb |
| Descriptor | Hypothetical protein ST2348 (2 entities in total) |
| Functional Keywords | cbs-domain, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, oxidoreductase |
| Biological source | Sulfolobus tokodaii |
| Total number of polymer chains | 2 |
| Total formula weight | 30293.00 |
| Authors | Agari, Y.,Karthe, P.,Kumarevel, T.,Yokoyama, S.,Kuramitsu, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2007-02-21, release date: 2007-08-21, Last modification date: 2024-11-13) |
| Primary citation | Ragunathan, P.,Kumarevel, T.,Agari, Y.,Shinkai, A.,Kuramitsu, S.,Yokoyama, S.,Ponnuraj, K. Crystal structure of ST2348, a CBS domain protein, from hyperthermophilic archaeon Sulfolobus tokodaii Biochem.Biophys.Res.Commun., 375:124-128, 2008 Cited by PubMed Abstract: The crystal structure of a hypothetical protein ST2348 (GI: 47118305) from the hyperthermophilic bacteria Sulfolobus tokodaii has been determined using X-ray crystallography. The protein consists of two CBS (cystathione beta synthase) domains, whose function has been analyzed and reported here. PSI-BLAST shows a conservation of this domain in about 100 proteins in various species. However, none of the close homologs of ST2348 have been functionally characterized so far. Structure and sequence comparison of ST2348 with human AMP-kinase gamma1 subunit and the CBS domain pair of bacterial IMP dehydrogenase is suggestive of its binding to AMP and ATP. A highly conserved residue Asp118, located in a negatively charged patch near the ligand binding cleft, could serve as a site for phosphorylation similar to that found in the chemotatic signal protein CheY and thereby ST2348 can function as a signal transduction molecule. PubMed: 18691556DOI: 10.1016/j.bbrc.2008.07.140 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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