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| {{STRUCTURE_2iy7| PDB=2iy7 | SCENE= }} | | {{STRUCTURE_2iy7| PDB=2iy7 | SCENE= }} |
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| '''CRYSTAL STRUCTURE OF THE SIALYLTRANSFERASE PM0188 WITH CMP-3FNEUAC'''
| | ===CRYSTAL STRUCTURE OF THE SIALYLTRANSFERASE PM0188 WITH CMP-3FNEUAC=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_18304450}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 18304450 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_18304450}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Sialyltransferase]] | | [[Category: Sialyltransferase]] |
| [[Category: Transferase]] | | [[Category: Transferase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 08:04:04 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:46:18 2008'' |