3s44

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==Crystal Structure of Pasteurella multocida sialyltransferase M144D mutant with CMP bound==
==Crystal Structure of Pasteurella multocida sialyltransferase M144D mutant with CMP bound==
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<StructureSection load='3s44' size='340' side='right' caption='[[3s44]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
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<StructureSection load='3s44' size='340' side='right'caption='[[3s44]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3s44]] is a 1 chain structure with 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=3S44 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3S44 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3s44]] 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=3S44 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3S44 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FN5:CMP-3F(A)-NEU5AC'>FN5</scene></td></tr>
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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]] 1.45&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ex1|2ex1]], [[2ihj|2ihj]], [[2ihk|2ihk]], [[2ihz|2ihz]], [[2ilv|2ilv]], [[2ex0|2ex0]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FN5:CMP-3F(A)-NEU5AC'>FN5</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">homologue of Pm0188 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=747 Pasteurella multocida])</td></tr>
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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=3s44 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s44 OCA], [https://pdbe.org/3s44 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3s44 RCSB], [https://www.ebi.ac.uk/pdbsum/3s44 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3s44 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3s44 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s44 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3s44 RCSB], [http://www.ebi.ac.uk/pdbsum/3s44 PDBsum]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q15KI8_PASMD Q15KI8_PASMD]
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Glycosyltransferases are important catalysts for enzymatic and chemoenzymatic synthesis of complex carbohydrates and glycoconjugates. The glycosylation efficiencies of wild-type glycosyltransferases vary considerably when different acceptor substrates are used. Using a multifunctional Pasteurella multocida sialyltransferase 1 (PmST1) as an example, we show here that the sugar nucleotide donor hydrolysis activity of glycosyltransferases contributes significantly to the low yield of glycosylation when a poor acceptor substrate is used. With a protein crystal structure-based rational design, we generated a single mutant (PmST1 M144D) with decreased donor hydrolysis activity without significantly affecting its alpha2-3-sialylation activity when a poor fucose-containing acceptor substrate was used. The single mutant also has a drastically decreased alpha2-3-sialidase activity. X-ray and NMR structural studies revealed that unlike the wild-type PmST1, which changes to a closed conformation once a donor binds, the M144D mutant structure adopts an open conformation even in the presence of the donor substrate. The PmST1 M144D mutant with decreased donor hydrolysis and reduced sialidase activity has been used as a powerful catalyst for efficient chemoenzymatic synthesis of complex sialyl Lewis(x) antigens containing different sialic acid forms. This work sheds new light on the effect of donor hydrolysis activity of glycosyltransferases on glycosyltransferase-catalyzed reactions and provides a novel strategy to improve glycosyltransferase substrate promiscuity by decreasing its donor hydrolysis activity.
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A Sialyltransferase Mutant with Decreased Donor Hydrolysis and Reduced Sialidase Activities for Directly Sialylating Lewis(x).,Sugiarto G, Lau K, Qu J, Li Y, Lim S, Mu S, Ames JB, Fisher AJ, Chen X ACS Chem Biol. 2012 Jul 20;7(7):1232-40. Epub 2012 May 14. PMID:22583967<ref>PMID:22583967</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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==See Also==
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</div>
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*[[Sialyltransferase 3D structures|Sialyltransferase 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Large Structures]]
[[Category: Pasteurella multocida]]
[[Category: Pasteurella multocida]]
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[[Category: Ames, J B]]
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[[Category: Ames JB]]
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[[Category: Chen, X]]
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[[Category: Chen X]]
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[[Category: Fisher, A J]]
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[[Category: Fisher AJ]]
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[[Category: Lau, K]]
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[[Category: Lau K]]
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[[Category: Le, D T]]
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[[Category: Le D-T]]
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[[Category: Li, Y]]
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[[Category: Li Y]]
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[[Category: Lim, S]]
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[[Category: Lim S]]
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[[Category: Sugiarto, G]]
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[[Category: Sugiarto G]]
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[[Category: Gt-b fold]]
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[[Category: Sialyltransferase]]
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[[Category: Transferase]]
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Current revision

Crystal Structure of Pasteurella multocida sialyltransferase M144D mutant with CMP bound

PDB ID 3s44

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