3cop

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "3cop" [edit=sysop:move=sysop])
Current revision (12:31, 30 August 2023) (edit) (undo)
 
(5 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:3cop.png|left|200px]]
 
-
{{STRUCTURE_3cop| PDB=3cop | SCENE= }}
+
==Crystal Structure of E.coli GS mutant E377A in complex with ADP and acceptor analogue HEPPSO==
 +
<StructureSection load='3cop' size='340' side='right'caption='[[3cop]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[3cop]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3COP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3COP 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]] 2.3&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=250:(2R)-2-HYDROXY-3-[4-(2-HYDROXYETHYL)PIPERAZIN-1-YL]PROPANE-1-SULFONIC+ACID'>250</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</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=3cop FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cop OCA], [https://pdbe.org/3cop PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cop RCSB], [https://www.ebi.ac.uk/pdbsum/3cop PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cop ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/GLGA_ECOLI GLGA_ECOLI] Synthesizes alpha-1,4-glucan chains using ADP-glucose.
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/co/3cop_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3cop ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Escherichia coli glycogen synthase (EcGS, EC 2.4.1.21) is a retaining glycosyltransferase (GT) that transfers glucose from adenosine diphosphate glucose to a glucan chain acceptor with retention of configuration at the anomeric carbon. EcGS belongs to the GT-B structural superfamily. Here we report several EcGS x-ray structures that together shed considerable light on the structure and function of these enzymes. The structure of the wild-type enzyme bound to ADP and glucose revealed a 15.2 degrees overall domain-domain closure and provided for the first time the structure of the catalytically active, closed conformation of a glycogen synthase. The main chain carbonyl group of His-161, Arg-300, and Lys-305 are suggested by the structure to act as critical catalytic residues in the transglycosylation. Glu-377, previously thought to be catalytic is found on the alpha-face of the glucose and plays an electrostatic role in the active site and as a glucose ring locator. This is also consistent with the structure of the EcGS(E377A)-ADP-HEPPSO complex where the glucose moiety is either absent or disordered in the active site.
-
===Crystal Structure of E.coli GS mutant E377A in complex with ADP and acceptor analogue HEPPSO===
+
The crystal structures of the open and catalytically competent closed conformation of Escherichia coli glycogen synthase.,Sheng F, Jia X, Yep A, Preiss J, Geiger JH J Biol Chem. 2009 Jun 26;284(26):17796-807. Epub 2009 Feb 25. PMID:19244233<ref>PMID:19244233</ref>
-
{{ABSTRACT_PUBMED_19244233}}
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
 
+
</div>
-
==About this Structure==
+
<div class="pdbe-citations 3cop" style="background-color:#fffaf0;"></div>
-
[[3cop]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3COP OCA].
+
== References ==
-
 
+
<references/>
-
==Reference==
+
__TOC__
-
<ref group="xtra">PMID:019244233</ref><references group="xtra"/>
+
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
-
[[Category: Starch synthase]]
+
[[Category: Large Structures]]
-
[[Category: Geiger, J H.]]
+
[[Category: Geiger JH]]
-
[[Category: Sheng, F.]]
+
[[Category: Sheng F]]
-
[[Category: Acceptor analogue heppso binding]]
+
-
[[Category: Adp]]
+
-
[[Category: Closed-form]]
+
-
[[Category: Glycogen biosynthesis]]
+
-
[[Category: Glycosyl-transferase]]
+
-
[[Category: Glycosyltransferase]]
+
-
[[Category: Gt-b fold]]
+
-
[[Category: Rossmann fold]]
+
-
[[Category: Transferase]]
+

Current revision

Crystal Structure of E.coli GS mutant E377A in complex with ADP and acceptor analogue HEPPSO

PDB ID 3cop

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3cop"
Personal tools