4fg4: Difference between revisions

Revision as of 04:55, 7 October 2022

Crystal structure of Bacillus Subtilis expansin (EXLX1) in complex with hemithiocellodextrin

Structural highlights

4fg4 is a 2 chain structure with sequence from Bacillus subtilis subsp. subtilis str. 168. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	BGC, GS1, PRD_900095, SGC
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

YOAJ_BACSU May promote colonization of plant roots. May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. Has very low expansin activity (in vitro). No enzymatic activity has been found. Binds to peptidoglycan and to plant cell walls.^[1]

Publication Abstract from PubMed

Components of modular cellulases, type-A cellulose-binding modules (CBMs) bind to crystalline cellulose and enhance enzyme effectiveness, but structural details of the interaction are uncertain. We analyzed cellulose binding by EXLX1, a bacterial expansin with ability to loosen plant cell walls and whose domain D2 has type-A CBM characteristics. EXLX1 strongly binds to crystalline cellulose via D2, whereas its affinity for soluble cellooligosaccharides is weak. Calorimetry indicated cellulose binding was largely entropically driven. We solved the crystal structures of EXLX1 complexed with cellulose-like oligosaccharides to find that EXLX1 binds the ligands through hydrophobic interactions of three linearly arranged aromatic residues in D2. The crystal structures revealed a unique form of ligand-mediated dimerization, with the oligosaccharide sandwiched between two D2 domains in opposite polarity. This report clarifies the molecular target of expansin and the specific molecular interactions of a type-A CBM with cellulose.

Structural basis for entropy-driven cellulose binding by a type-A cellulose-binding module (CBM) and bacterial expansin.,Georgelis N, Yennawar NH, Cosgrove DJ Proc Natl Acad Sci U S A. 2012 Sep 11;109(37):14830-5. Epub 2012 Aug 27. PMID:22927418^[2]

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

References

↑ Kerff F, Amoroso A, Herman R, Sauvage E, Petrella S, Filee P, Charlier P, Joris B, Tabuchi A, Nikolaidis N, Cosgrove DJ. Crystal structure and activity of Bacillus subtilis YoaJ (EXLX1), a bacterial expansin that promotes root colonization. Proc Natl Acad Sci U S A. 2008 Nov 4;105(44):16876-81. Epub 2008 Oct 29. PMID:18971341
↑ Georgelis N, Yennawar NH, Cosgrove DJ. Structural basis for entropy-driven cellulose binding by a type-A cellulose-binding module (CBM) and bacterial expansin. Proc Natl Acad Sci U S A. 2012 Sep 11;109(37):14830-5. Epub 2012 Aug 27. PMID:22927418 doi:https://dx.doi.org/10.1073/pnas.1213200109

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OCA

[1] Kerff F, Amoroso A, Herman R, Sauvage E, Petrella S, Filee P, Charlier P, Joris B, Tabuchi A, Nikolaidis N, Cosgrove DJ. Crystal structure and activity of Bacillus subtilis YoaJ (EXLX1), a bacterial expansin that promotes root colonization. Proc Natl Acad Sci U S A. 2008 Nov 4;105(44):16876-81. Epub 2008 Oct 29. PMID:18971341

[2] Georgelis N, Yennawar NH, Cosgrove DJ. Structural basis for entropy-driven cellulose binding by a type-A cellulose-binding module (CBM) and bacterial expansin. Proc Natl Acad Sci U S A. 2012 Sep 11;109(37):14830-5. Epub 2012 Aug 27. PMID:22927418 doi:https://dx.doi.org/10.1073/pnas.1213200109

[1]

[2]

@@ Line 1: / Line 1: @@
 ==Crystal structure of Bacillus Subtilis expansin (EXLX1) in complex with hemithiocellodextrin==
-<StructureSection load='4fg4' size='340' side='right' caption='[[4fg4]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
+<StructureSection load='4fg4' size='340' side='right'caption='[[4fg4]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4fg4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacsu Bacsu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FG4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FG4 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4fg4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FG4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FG4 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0TS:BETA-D-GLUCOPYRANOSYL-(1- 4)-4-THIO-BETA-D-GLUCOPYRANOSYL-(1- 4)-BETA-D-GLUCOPYRANOSYL-(1- 4)-4-THIO-BETA-D-GLUCOPYRANOSYL-(1- 4)-1-THIO-BETA-D-GLUCOPYRANOSE'>0TS</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GS1:1-THIO-BETA-D-GLUCOPYRANOSE'>GS1</scene>, <scene name='pdbligand=PRD_900095:hemithiocellodextrin'>PRD_900095</scene>, <scene name='pdbligand=SGC:4-DEOXY-4-THIO-BETA-D-GLUCOPYRANOSE'>SGC</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4fer|4fer]], [[4fft|4fft]], [[4fg2|4fg2]], [[3d30|3d30]], [[2bh0|2bh0]]</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=4fg4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fg4 OCA], [https://pdbe.org/4fg4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fg4 RCSB], [https://www.ebi.ac.uk/pdbsum/4fg4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fg4 ProSAT]</span></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">yoaJ, BSU18630 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</td></tr>
-<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=4fg4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fg4 OCA], [http://pdbe.org/4fg4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fg4 RCSB], [http://www.ebi.ac.uk/pdbsum/4fg4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fg4 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/YOAJ_BACSU YOAJ_BACSU]] May promote colonization of plant roots. May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. Has very low expansin activity (in vitro). No enzymatic activity has been found. Binds to peptidoglycan and to plant cell walls.<ref>PMID:18971341</ref>
+[https://www.uniprot.org/uniprot/YOAJ_BACSU YOAJ_BACSU] May promote colonization of plant roots. May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. Has very low expansin activity (in vitro). No enzymatic activity has been found. Binds to peptidoglycan and to plant cell walls.<ref>PMID:18971341</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 24: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Bacsu]]
+[[Category: Bacillus subtilis subsp. subtilis str. 168]]
-[[Category: Cosgrove, D J]]
+[[Category: Large Structures]]
-[[Category: Georgelis, N]]
+[[Category: Cosgrove DJ]]
-[[Category: Yennawar, N H]]
+[[Category: Georgelis N]]
-[[Category: Cellulose]]
+[[Category: Yennawar NH]]
-[[Category: Cellulose-binding protein]]

4fg4: Difference between revisions

Revision as of 04:55, 7 October 2022

Crystal structure of Bacillus Subtilis expansin (EXLX1) in complex with hemithiocellodextrin

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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