2iy8

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|PDB= 2iy8 |SIZE=350|CAPTION= <scene name='initialview01'>2iy8</scene>, resolution 2.5&Aring;
|PDB= 2iy8 |SIZE=350|CAPTION= <scene name='initialview01'>2iy8</scene>, resolution 2.5&Aring;
|SITE= <scene name='pdbsite=AC1:Lat+Binding+Site+For+Chain+A'>AC1</scene> and <scene name='pdbsite=AC2:Csf+Binding+Site+For+Chain+A'>AC2</scene>
|SITE= <scene name='pdbsite=AC1:Lat+Binding+Site+For+Chain+A'>AC1</scene> and <scene name='pdbsite=AC2:Csf+Binding+Site+For+Chain+A'>AC2</scene>
-
|LIGAND= <scene name='pdbligand=LAT:LACTOSE'>LAT</scene> and <scene name='pdbligand=CSF:CYTIDINE-5&#39;-MONOPHOSPHATE-3-FLUORO-N-ACETYL-NEURAMINIC ACID'>CSF</scene>
+
|LIGAND= <scene name='pdbligand=CSF:CYTIDINE-5&#39;-MONOPHOSPHATE-3-FLUORO-N-ACETYL-NEURAMINIC+ACID'>CSF</scene>, <scene name='pdbligand=LAT:LACTOSE'>LAT</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
 +
|DOMAIN=
 +
|RELATEDENTRY=[[2c83|2C83]], [[2c84|2C84]], [[2ex0|2EX0]], [[2ex1|2EX1]], [[2iy7|2IY7]]
 +
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2iy8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iy8 OCA], [http://www.ebi.ac.uk/pdbsum/2iy8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2iy8 RCSB]</span>
}}
}}
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[[Category: Cho, H S.]]
[[Category: Cho, H S.]]
[[Category: Kim, D U.]]
[[Category: Kim, D U.]]
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[[Category: CSF]]
 
-
[[Category: LAT]]
 
[[Category: cmp-3fneuac]]
[[Category: cmp-3fneuac]]
[[Category: hypothetical protein]]
[[Category: hypothetical protein]]
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[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 15:23:13 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:50:27 2008''

Revision as of 00:50, 31 March 2008


PDB ID 2iy8

Drag the structure with the mouse to rotate
, resolution 2.5Å
Sites: and
Ligands: , ,
Related: 2C83, 2C84, 2EX0, 2EX1, 2IY7


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF THE SIALYLTRANSFERASE PM0188 WITH CMP-3FNEUAC AND LACTOSE


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

2IY8 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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