2iy7: Difference between revisions

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-[[Image:2iy7.jpg|left|200px]]
- {{Structure
+==crystal structure of the sialyltransferase PM0188 with CMP-3FNeuAc==
-|PDB= 2iy7 |SIZE=350|CAPTION= <scene name='initialview01'>2iy7</scene>, resolution 1.85&Aring;
+<StructureSection load='2iy7' size='340' side='right'caption='[[2iy7]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
-|SITE= <scene name='pdbsite=AC1:Csf+Binding+Site+For+Chain+A'>AC1</scene>
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=CSF:CYTIDINE-5&#39;-MONOPHOSPHATE-3-FLUORO-N-ACETYL-NEURAMINIC ACID'>CSF</scene>
+<table><tr><td colspan='2'>[[2iy7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pasteurella_multocida Pasteurella multocida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IY7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IY7 FirstGlance]. <br>
-|ACTIVITY=
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
-|GENE=
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSF:CYTIDINE-5-MONOPHOSPHATE-3-FLUORO-N-ACETYL-NEURAMINIC+ACID'>CSF</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-}}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2iy7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iy7 OCA], [https://pdbe.org/2iy7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iy7 RCSB], [https://www.ebi.ac.uk/pdbsum/2iy7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iy7 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q15KI8_PASMD Q15KI8_PASMD]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-'''CRYSTAL STRUCTURE OF THE SIALYLTRANSFERASE PM0188 WITH CMP-3FNEUAC'''
+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<ref>PMID:18304450</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2iy7" style="background-color:#fffaf0;"></div>
-==Overview==
+==See Also==
-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.
+*[[Sialyltransferase 3D structures|Sialyltransferase 3D structures]]
+== References ==
-==About this Structure==
+<references/>
-IY7 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=2IY7 OCA].
+__TOC__
+</StructureSection>
-==Reference==
+[[Category: Large Structures]]
-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: Single protein]]
+[[Category: Cho HS]]
-[[Category: Cho, H S.]]
+[[Category: Kim DU]]
-[[Category: Kim, D U.]]
-[[Category: CSF]]
-[[Category: cmp-3fneuac]]
-[[Category: hypothetical protein]]
-[[Category: sialyltransferase]]
-[[Category: transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 15:23:12 2008''