| Title | Crystal structure of Periplasmic divalent cation tolerance protein (TM1056) from Thermotoga maritima at 1.95 A resolution. To be published | | Site | JCSG | | PDB Id | | Target Id | 282923 | | Molecular Characteristics | | Source | Thermotoga maritima msb8 | | Alias Ids | TPS1257,TM1056 | Molecular Weight | 12176.50 Da. | | Residues | 101 | Isoelectric Point | 5.30 | | Sequence | milvystfpneekaleigrkllekrliacfnafeirsgywwkgeivqdkewaaifktteekekelyeel rklhpyetpaiftlkvenvlteymnwlresvl | | | BLAST FFAS | | Structure Determination | | Method | XRAY | Chains | 1 | | Resolution (Å) | 1.95 | Rfree | 0.22061 | | Matthews' coefficent | 2.05 | Rfactor | 0.15603 | | Waters | 74 | Solvent Content | 39.45 |
| Ligand Information | | Ligands | | | Metals | | | |
Protein Summary
The gene TM1056 from Thermotoga maritima encodes a protein CutA (CutA1 superfamily) involved in divalent metal tolerance PF03091 . The structure of Thermotoga CutA has been solved previously 1KR4. CutA1 can be found in bacteria, plants, animals and humans [Ref] . The protein was originally identified in a gene locus cutA of Escherichia coli [Ref] . Several of CutA1 homologue have been crystallized previously (1VHF, E.Coli; 2E66, Pyrococcus Horikoshii). In these structures CutA1 protein is a trimer. Molecular genetics studies on the E. coli cutA locus showed that some mutations lead to copper sensitivity due to its increased uptake [Ref] . CutA1 may be involved in the tuning of a disulphide bond cascade in bacteria and mammals, acting as the PII proteins do in the nitrogen signal cascade in bacteria and plants.
Ligand Summary
References
