Summary for 1SR3
| Entry DOI | 10.2210/pdb1sr3/pdb |
| Descriptor | APO-CCME (1 entity in total) |
| Functional Keywords | ob fold, beta barrel, flexible c-terminal domain, chaperone |
| Biological source | Escherichia coli |
| Cellular location | Cell inner membrane; Single-pass type II membrane protein; Periplasmic side (Potential): P69490 |
| Total number of polymer chains | 1 |
| Total formula weight | 15349.21 |
| Authors | Enggist, E.,Thony-Meyer, L.,Guntert, P.,Pervushin, K. (deposition date: 2004-03-22, release date: 2004-04-06, Last modification date: 2024-05-29) |
| Primary citation | Enggist, E.,Thony-Meyer, L.,Guntert, P.,Pervushin, K. NMR Structure of the Heme Chaperone Ccme Reveals a Novel Functional Motif Structure, 10:1551-1557, 2002 Cited by PubMed Abstract: The concept of metal chaperones involves transient binding of metallic cofactors by specific proteins for delivery to enzymes in which they function. Metal chaperones thus provide a protective, as well as a transport, function. We report the first structure of a heme chaperone, CcmE, which comprises these two functions. We propose that the covalent attachment of heme to an exposed histidine occurs after heme binding at the surface of a rigid molecule with a flexible C-terminal domain. CcmE belongs to a family of proteins with a specific fold, which all share a function in delivery of specific molecular cargo. PubMed: 12429096DOI: 10.1016/S0969-2126(02)00885-7 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
