2c83: Difference between revisions

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[[Image:2c83.png|left|200px]]


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==CRYSTAL STRUCTURE OF THE SIALYLTRANSFERASE PM0188==
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<StructureSection load='2c83' size='340' side='right'caption='[[2c83]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</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=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
{{STRUCTURE_2c83|  PDB=2c83  |  SCENE=  }}
<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.


===CRYSTAL STRUCTURE OF THE SIALYLTRANSFERASE PM0188===
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>
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== References ==
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<references/>
{{ABSTRACT_PUBMED_18304450}}
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</StructureSection>
==About this Structure==
[[Category: Large Structures]]
2C83 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=2C83 OCA].
 
==Reference==
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]
 
Structural analysis of the sialyltransferase CstII from Campylobacter jejuni in complex with a substrate analog., Chiu CP, Watts AG, Lairson LL, Gilbert M, Lim D, Wakarchuk WW, Withers SG, Strynadka NC, Nat Struct Mol Biol. 2004 Feb;11(2):163-70. Epub 2004 Jan 18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14730352 14730352]
 
Crystallization and preliminary X-ray crystallographic analysis of the alpha-2,6-sialyltransferase PM0188 from Pasteurella multosida., Kim DU, Yoo JH, Ryu K, Cho HS, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Feb 1;62(Pt, 2):142-4. Epub 2006 Jan 27. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16511286 16511286]
[[Category: Pasteurella multocida]]
[[Category: Pasteurella multocida]]
[[Category: Single protein]]
[[Category: Cho HS]]
[[Category: Cho, H S.]]
[[Category: Kim DU]]
[[Category: Kim, D U.]]
[[Category: Hypothetical protein]]
[[Category: Pm0188]]
[[Category: Sialyltransferase]]
[[Category: Transferase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:21:57 2008''

Latest revision as of 16:04, 26 July 2023

CRYSTAL STRUCTURE OF THE SIALYLTRANSFERASE PM0188CRYSTAL STRUCTURE OF THE SIALYLTRANSFERASE PM0188

Structural highlights

2c83 is a 1 chain structure with sequence from Pasteurella multocida. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q15KI8_PASMD

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Kim DU, Yoo JH, Lee YJ, Kim KS, Cho HS. Structural analysis of sialyltransferase PM0188 from Pasteurella multocida complexed with donor analogue and acceptor sugar. BMB Rep. 2008 Jan 31;41(1):48-54. PMID:18304450

2c83, resolution 1.90Å

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