2c83: Difference between revisions
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{{STRUCTURE_2c83| PDB=2c83 | SCENE= }} | |||
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'''CRYSTAL STRUCTURE OF THE SIALYLTRANSFERASE PM0188''' | '''CRYSTAL STRUCTURE OF THE SIALYLTRANSFERASE PM0188''' | ||
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[[Category: Cho, H S.]] | [[Category: Cho, H S.]] | ||
[[Category: Kim, D U.]] | [[Category: Kim, D U.]] | ||
[[Category: | [[Category: Hypothetical protein]] | ||
[[Category: | [[Category: Pm0188]] | ||
[[Category: | [[Category: Sialyltransferase]] | ||
[[Category: | [[Category: Transferase]] | ||
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Revision as of 21:25, 3 May 2008
CRYSTAL STRUCTURE OF THE SIALYLTRANSFERASE PM0188
OverviewOverview
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.
About this StructureAbout this Structure
2C83 is a Single protein structure of sequence from Pasteurella multocida. Full crystallographic information is available from OCA.
ReferenceReference
Structural analysis of sialyltransferase PM0188 from Pasteurella multocida complexed with donor analogue and acceptor sugar., Kim DU, Yoo JH, Lee YJ, Kim KS, Cho HS, BMB Rep. 2008 Jan 31;41(1):48-54. PMID:18304450 Page seeded by OCA on Sat May 3 21:25:34 2008