2IY7

crystal structure of the sialyltransferase PM0188 with CMP-3FNeuAc

Summary for 2IY7

• Entry DOI: 10.2210/pdb2iy7/pdb
• Related: 2C83 2C84 2EX0 2EX1 2IY8
• Descriptor: LPHA-2,3/2,6-SIALYLTRANSFERASE/SIALIDASE, CYTIDINE-5'-MONOPHOSPHATE-3-FLUORO-N-ACETYL-NEURAMINIC ACID (3 entities in total)
• Functional Keywords: sialyltransferase, cmp-3fneuac, transferase, hypothetical protein
• Biological source: PASTEURELLA MULTOCIDA
• Total number of polymer chains: 1
• Total formula weight: 46166.93

Authors

Kim, D.U.,Cho, H.S. (deposition date: 2006-07-13, release date: 2007-08-21, Last modification date: 2024-11-06)

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

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: 18304450
DOI: 10.5483/bmbrep.2008.41.1.048

Experimental method

X-RAY DIFFRACTION (1.85 Å)