2c84
From Proteopedia
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| - | [[Image:2c84.gif|left|200px]] | + | [[Image:2c84.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF THE SIALYLTRANSFERASE PM0188 WITH CMP''' | + | {{Structure |
| + | |PDB= 2c84 |SIZE=350|CAPTION= <scene name='initialview01'>2c84</scene>, resolution 2.31Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Binding+Site+For+Residue+C+A+1414'>AC1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=C:CYTIDINE-5'-MONOPHOSPHATE'>C</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF THE SIALYLTRANSFERASE PM0188 WITH CMP''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2C84 is a [ | + | 2C84 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pasteurella_multocida Pasteurella multocida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C84 OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/18304450 18304450] |
[[Category: Pasteurella multocida]] | [[Category: Pasteurella multocida]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:12:06 2008'' |
Revision as of 14:12, 20 March 2008
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| , resolution 2.31Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE SIALYLTRANSFERASE PM0188 WITH CMP
Overview
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 Structure
2C84 is a Single protein structure of sequence from Pasteurella multocida. Full crystallographic information is available from OCA.
Reference
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
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