3EKI
Structural insights of the Mycoplasma hyorhinis protein Mh-p37: A putative thiamine pyrophosphate transporter
Summary for 3EKI
| Entry DOI | 10.2210/pdb3eki/pdb |
| Related | 3E78 3E79 |
| Descriptor | High affinity transport system protein p37, THIAMINE DIPHOSPHATE, GLYCEROL, ... (6 entities in total) |
| Functional Keywords | mycoplasma, p37, tpp, cell membrane, lipoprotein, membrane, transport, transport protein, palmitate, extracytoplasmic thiamine binding lipoprotein, cypl, tpp binding protein |
| Biological source | Mycoplasma hyorhinis |
| Cellular location | Cell membrane; Lipid-anchor: P15363 |
| Total number of polymer chains | 1 |
| Total formula weight | 47274.71 |
| Authors | Sippel, K.H.,Robbins, A.H.,Reutzel, R.,McKenna, R. (deposition date: 2008-09-19, release date: 2009-06-23, Last modification date: 2023-08-30) |
| Primary citation | Sippel, K.H.,Robbins, A.H.,Reutzel, R.,Boehlein, S.K.,Namiki, K.,Goodison, S.,Agbandje-McKenna, M.,Rosser, C.J.,McKenna, R. Structural insights into the extracytoplasmic thiamine-binding lipoprotein p37 of Mycoplasma hyorhinis J.Bacteriol., 191:2585-2592, 2009 Cited by PubMed Abstract: The Mycoplasma hyorhinis protein p37 has been implicated in tumorigenic transformation for more than 20 years. Though there are many speculations as to its function, based solely on sequence homology, the issue has remained unresolved. Presented here is the 1.6-A-resolution refined crystal structure of M. hyorhinis p37, renamed the extracytoplasmic thiamine-binding lipoprotein (Cypl). The structure shows thiamine pyrophosphate (TPP) and two calcium ions are bound to Cypl and give the first insights into possible functions of the Cypl-like family of proteins. Sequence alignments of Cypl-like proteins between several different species of mycoplasma show that the thiamine-binding site is likely conserved and structural alignments reveal the similarity of Cypl to various binding proteins. While the experimentally determined function of Cypl remains unknown, the structure shows that the protein is a TPP-binding protein, opening up many avenues for future mechanistic studies and making Cypl a possible target for combating mycoplasma infections and tumorigenic transformation. PubMed: 19233924DOI: 10.1128/JB.01680-08 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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