2w61

From Proteopedia

(Difference between revisions)

Current revision

Saccharomyces cerevisiae Gas2p apostructure (E176Q mutant)

Structural highlights

2w61 is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.62Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GAS2_YEAST Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall. Involved in spore wall assembly.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Yeast cell wall remodeling is controlled by the equilibrium between glycoside hydrolases, glycosyltransferases, and transglycosylases. Family 72 glycoside hydrolases (GH72) are ubiquitous in fungal organisms and are known to possess significant transglycosylase activity, producing elongated beta(1-3) glucan chains. However, the molecular mechanisms that control the balance between hydrolysis and transglycosylation in these enzymes are not understood. Here we present the first crystal structure of a glucan transglycosylase, Saccharomyces cerevisiae Gas2 (ScGas2), revealing a multidomain fold, with a (betaalpha)(8) catalytic core and a separate glucan binding domain with an elongated, conserved glucan binding groove. Structures of ScGas2 complexes with different beta-glucan substrate/product oligosaccharides provide "snapshots" of substrate binding and hydrolysis/transglycosylation giving the first insights into the mechanisms these enzymes employ to drive beta(1-3) glucan elongation. Together with mutagenesis and analysis of reaction products, the structures suggest a "base occlusion" mechanism through which these enzymes protect the covalent protein-enzyme intermediate from a water nucleophile, thus controlling the balance between hydrolysis and transglycosylation and driving the elongation of beta(1-3) glucan chains in the yeast cell wall.

Molecular mechanisms of yeast cell wall glucan remodeling.,Hurtado-Guerrero R, Schuttelkopf AW, Mouyna I, Ibrahim AF, Shepherd S, Fontaine T, Latge JP, van Aalten DM J Biol Chem. 2009 Mar 27;284(13):8461-9. Epub 2008 Dec 19. PMID:19097997^[3]

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

References

↑ Ragni E, Coluccio A, Rolli E, Rodriguez-Pena JM, Colasante G, Arroyo J, Neiman AM, Popolo L. GAS2 and GAS4, a pair of developmentally regulated genes required for spore wall assembly in Saccharomyces cerevisiae. Eukaryot Cell. 2007 Feb;6(2):302-16. Epub 2006 Dec 22. PMID:17189486 doi:http://dx.doi.org/EC.00321-06
↑ Ragni E, Fontaine T, Gissi C, Latge JP, Popolo L. The Gas family of proteins of Saccharomyces cerevisiae: characterization and evolutionary analysis. Yeast. 2007 Apr;24(4):297-308. PMID:17397106 doi:http://dx.doi.org/10.1002/yea.1473
↑ Hurtado-Guerrero R, Schuttelkopf AW, Mouyna I, Ibrahim AF, Shepherd S, Fontaine T, Latge JP, van Aalten DM. Molecular mechanisms of yeast cell wall glucan remodeling. J Biol Chem. 2009 Mar 27;284(13):8461-9. Epub 2008 Dec 19. PMID:19097997 doi:10.1074/jbc.M807990200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2w61"

Categories: Large Structures | Saccharomyces cerevisiae | Hurtado-Guerrero R | Schuettelkopf AW | Van Aalten DMF

@@ Line 3: / Line 3: @@
 <StructureSection load='2w61' size='340' side='right'caption='[[2w61]], [[Resolution|resolution]] 1.62&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2w61]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W61 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W61 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2w61]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W61 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W61 FirstGlance]. <br>
-</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=2w61 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w61 OCA], [https://pdbe.org/2w61 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2w61 RCSB], [https://www.ebi.ac.uk/pdbsum/2w61 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2w61 ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.62&#8491;</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=2w61 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w61 OCA], [https://pdbe.org/2w61 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2w61 RCSB], [https://www.ebi.ac.uk/pdbsum/2w61 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2w61 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/GAS2_YEAST GAS2_YEAST]] Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall. Involved in spore wall assembly.<ref>PMID:17189486</ref> <ref>PMID:17397106</ref>
+[https://www.uniprot.org/uniprot/GAS2_YEAST GAS2_YEAST] Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall. Involved in spore wall assembly.<ref>PMID:17189486</ref> <ref>PMID:17397106</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 13: / Line 14: @@
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w6/2w61_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 31: / Line 32: @@
 __TOC__
 </StructureSection>
-[[Category: Atcc 18824]]
 [[Category: Large Structures]]
-[[Category: Aalten, D M.F van]]
+[[Category: Saccharomyces cerevisiae]]
-[[Category: Hurtado-Guerrero, R]]
+[[Category: Hurtado-Guerrero R]]
-[[Category: Schuettelkopf, A W]]
+[[Category: Schuettelkopf AW]]
-[[Category: Cell membrane]]
+[[Category: Van Aalten DMF]]
-[[Category: Fungal cell wall]]
-[[Category: Glucan]]
-[[Category: Glycoprotein]]
-[[Category: Gpi-anchor]]
-[[Category: Lipoprotein]]
-[[Category: Membrane]]
-[[Category: Transglycosylation]]

2w61

From Proteopedia

Current revision

Saccharomyces cerevisiae Gas2p apostructure (E176Q mutant)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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