2C84
CRYSTAL STRUCTURE OF THE SIALYLTRANSFERASE PM0188 WITH CMP
Summary for 2C84
| Entry DOI | 10.2210/pdb2c84/pdb |
| Related | 2C83 |
| Descriptor | ALPHA-2,3/2,6-SIALYLTRANSFERASE/SIALIDASE, CYTIDINE-5'-MONOPHOSPHATE (3 entities in total) |
| Functional Keywords | hypothetical protein, pm0188, sialyltransferase, cmp, transferase, glycosyltransferase |
| Biological source | Pasteurella multocida |
| Total number of polymer chains | 1 |
| Total formula weight | 45857.68 |
| Authors | |
| Primary citation | Kim, D.U.,Yoo, J.H.,Lee, Y.J.,Kim, K.S.,Cho, H.S. Structural analysis of sialyltransferase PM0188 from Pasteurella multocida complexed with donor analogue and acceptor sugar. Bmb Rep, 41:48-54, 2008 Cited by PubMed Abstract: PM0188 is a newly identified sialyltransferase from P. multocida which transfers sialic acid from cytidine 5'-monophosphonuraminic acid (CMP-NeuAc) to an acceptor sugar. Although sialyltransferases are involved in important biological functions like cell-cell recognition, cell differentiation and receptor-ligand interactions, little is known about their catalytic mechanism. Here, we report the X-ray crystal structures of PM0188 in the presence of an acceptor sugar and a donor sugar analogue, revealing the precise mechanism of sialic acid transfer. Site-directed mutagenesis, kinetic assays, and structural analysis show that Asp141, His311, Glu338, Ser355 and Ser356 are important catalytic residues; Asp141 is especially crucial as it acts as a general base. These complex structures provide insights into the mechanism of sialyltransferases and the structure-based design of specific inhibitors. PubMed: 18304450DOI: 10.5483/bmbrep.2008.41.1.048 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.31 Å) |
Structure validation
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