2iy7

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 4: Line 4:
|PDB= 2iy7 |SIZE=350|CAPTION= <scene name='initialview01'>2iy7</scene>, resolution 1.85&Aring;
|PDB= 2iy7 |SIZE=350|CAPTION= <scene name='initialview01'>2iy7</scene>, resolution 1.85&Aring;
|SITE= <scene name='pdbsite=AC1:Csf+Binding+Site+For+Chain+A'>AC1</scene>
|SITE= <scene name='pdbsite=AC1:Csf+Binding+Site+For+Chain+A'>AC1</scene>
-
|LIGAND= <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=MSE:SELENOMETHIONINE'>MSE</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
 +
|DOMAIN=
 +
|RELATEDENTRY=[[2c83|2C83]], [[2c84|2C84]], [[2ex0|2EX0]], [[2ex1|2EX1]], [[2iy8|2IY8]]
 +
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2iy7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iy7 OCA], [http://www.ebi.ac.uk/pdbsum/2iy7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2iy7 RCSB]</span>
}}
}}
Line 24: Line 27:
[[Category: Cho, H S.]]
[[Category: Cho, H S.]]
[[Category: Kim, D U.]]
[[Category: Kim, D U.]]
-
[[Category: CSF]]
 
[[Category: cmp-3fneuac]]
[[Category: cmp-3fneuac]]
[[Category: hypothetical protein]]
[[Category: hypothetical protein]]
Line 30: Line 32:
[[Category: transferase]]
[[Category: transferase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 15:23:12 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:50:22 2008''

Revision as of 00:50, 31 March 2008


PDB ID 2iy7

Drag the structure with the mouse to rotate
, resolution 1.85Å
Sites:
Ligands: ,
Related: 2C83, 2C84, 2EX0, 2EX1, 2IY8


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



CRYSTAL STRUCTURE OF THE SIALYLTRANSFERASE PM0188 WITH CMP-3FNEUAC


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

2IY7 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

Page seeded by OCA on Mon Mar 31 03:50:22 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools