This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.




2c83

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (13:04, 26 July 2023) (edit) (undo)
 
(10 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2c83.gif|left|200px]]
 
-
<!--
+
==CRYSTAL STRUCTURE OF THE SIALYLTRANSFERASE PM0188==
-
The line below this paragraph, containing "STRUCTURE_2c83", creates the "Structure Box" on the page.
+
<StructureSection load='2c83' size='340' side='right'caption='[[2c83]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== 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>
-
-->
+
<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>
-
'''CRYSTAL STRUCTURE OF THE SIALYLTRANSFERASE PM0188'''
+
== Function ==
-
 
+
[https://www.uniprot.org/uniprot/Q15KI8_PASMD Q15KI8_PASMD]
-
 
+
<div style="background-color:#fffaf0;">
-
==Overview==
+
== 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.
-
==About this Structure==
+
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>
-
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==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
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]
+
</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: 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 Sat May 3 21:25:34 2008''
+

Current revision

CRYSTAL STRUCTURE OF THE SIALYLTRANSFERASE PM0188

PDB ID 2c83

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools