2c83: Difference between revisions
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== | ==CRYSTAL STRUCTURE OF THE SIALYLTRANSFERASE PM0188== | ||
<StructureSection load='2c83' size='340' side='right'caption='[[2c83]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2c83]] 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=2C83 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C83 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]] 1.9Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=2c83 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c83 OCA], [https://pdbe.org/2c83 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c83 RCSB], [https://www.ebi.ac.uk/pdbsum/2c83 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c83 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. | 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 2c83" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Pasteurella multocida]] | [[Category: Pasteurella multocida]] | ||
[[Category: Cho HS]] | |||
[[Category: Cho | [[Category: Kim DU]] | ||
[[Category: Kim | |||
Latest revision as of 16:04, 26 July 2023
CRYSTAL STRUCTURE OF THE SIALYLTRANSFERASE PM0188CRYSTAL STRUCTURE OF THE SIALYLTRANSFERASE PM0188
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. References |
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