2iy7: Difference between revisions
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==crystal structure of the sialyltransferase PM0188 with CMP-3FNeuAc== | |||
<StructureSection load='2iy7' size='340' side='right'caption='[[2iy7]], [[Resolution|resolution]] 1.85Å' scene=''> | |||
== Structural highlights == | |||
<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> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85Å</td></tr> | |||
<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. | |||
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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2iy7" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
[[ | *[[Sialyltransferase 3D structures|Sialyltransferase 3D structures]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Pasteurella multocida]] | [[Category: Pasteurella multocida]] | ||
[[Category: Cho | [[Category: Cho HS]] | ||
[[Category: Kim | [[Category: Kim DU]] | ||
Latest revision as of 16:07, 26 July 2023
crystal structure of the sialyltransferase PM0188 with CMP-3FNeuAccrystal structure of the sialyltransferase PM0188 with CMP-3FNeuAc
Structural highlights
FunctionPublication Abstract from PubMedPM0188 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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