2OQ3
Solution Structure of the mannitol- specific cryptic phosphotransferase enzyme IIA CmtB from Escherichia coli
Summary for 2OQ3
| Entry DOI | 10.2210/pdb2oq3/pdb |
| NMR Information | BMRB: 15126 |
| Descriptor | Mannitol-specific cryptic phosphotransferase enzyme IIA component (1 entity in total) |
| Functional Keywords | mannitol, phosphotransferase, escherichia coli, solution structure, transferase |
| Biological source | Escherichia coli |
| Cellular location | Cytoplasm (Probable): P69824 |
| Total number of polymer chains | 1 |
| Total formula weight | 16340.43 |
| Authors | |
| Primary citation | Yu, C.,Li, Y.,Xia, B.,Jin, C. Solution structure of the cryptic mannitol-specific phosphotransferase enzyme IIA CmtB from Escherichia coli Biochem.Biophys.Res.Commun., 362:1001-1006, 2007 Cited by PubMed Abstract: The bacterial phosphoenolpyruvate-dependent sugar phosphotransferase system (PEP-PTS) is essential in the coupled transportation and phosphorylation of various types of carbohydrates. The CmtAB proteins of Escherichia coli are sequentially similar to the mannitol-specific phosphotransferase MtlA. The CmtB protein corresponds to the phosphotransferase enzyme IIA component. Here we report the solution structure of CmtB from E. coli at high resolution by NMR spectroscopy. The results show that CmtB adopts a globular fold consisting of a central mixed five-strand beta-sheet flanked by seven helices at both sides. Structural comparison with the IIA domain of MtlA (IIAMtl) reveals high overall similarity, while notable conformational differences at the active site are observed. The active site pocket of CmtB appears to be wider, and the hydrophobic regions around it is larger compared to IIAMtl. Further, the essential arginine residue at the active site of IIAMtl is substituted by a serine in CmtB. Instead, the active pocket of CmtB contains another arginine at a distinct position, suggesting different molecular mechanisms for phosphoryl transfer. PubMed: 17803963DOI: 10.1016/j.bbrc.2007.08.102 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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