2iy8

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[[Image:2iy8.jpg|left|200px]]
 
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{{Structure
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==Crystal structure of the sialyltransferase PM0188 with CMP-3FNeuAc and lactose==
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|PDB= 2iy8 |SIZE=350|CAPTION= <scene name='initialview01'>2iy8</scene>, resolution 2.5&Aring;
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<StructureSection load='2iy8' size='340' side='right'caption='[[2iy8]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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|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>
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== Structural highlights ==
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|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>
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<table><tr><td colspan='2'>[[2iy8]] 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=2IY8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IY8 FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CSF:CYTIDINE-5-MONOPHOSPHATE-3-FLUORO-N-ACETYL-NEURAMINIC+ACID'>CSF</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PRD_900004:beta-lactose'>PRD_900004</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2iy8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iy8 OCA], [https://pdbe.org/2iy8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iy8 RCSB], [https://www.ebi.ac.uk/pdbsum/2iy8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iy8 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q9CP67_PASMU Q9CP67_PASMU]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''CRYSTAL STRUCTURE OF THE SIALYLTRANSFERASE PM0188 WITH CMP-3FNEUAC AND LACTOSE'''
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2iy8" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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.
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*[[Sialyltransferase 3D structures|Sialyltransferase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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2IY8 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=2IY8 OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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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]
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[[Category: Pasteurella multocida]]
[[Category: Pasteurella multocida]]
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[[Category: Single protein]]
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[[Category: Cho HS]]
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[[Category: Cho, H S.]]
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[[Category: Kim DU]]
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[[Category: Kim, D U.]]
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[[Category: CSF]]
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[[Category: LAT]]
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[[Category: cmp-3fneuac]]
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[[Category: hypothetical protein]]
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[[Category: lactose]]
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[[Category: pm0188]]
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[[Category: sialyltransferase]]
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[[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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Current revision

Crystal structure of the sialyltransferase PM0188 with CMP-3FNeuAc and lactose

PDB ID 2iy8

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