6g1g: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

~~The entry~~ 6g1g is ~~ON HOLD until Paper~~ Publication

==GH124 cellulase from Ruminiclostridium thermocellum in complex with Mn and cellotriose==

== Structural highlights ==

<table><tr><td colspan='2'>[[6g1g]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6G1G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6G1G FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>

<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=OHI:3-(2-OXO-2H-IMIDAZOL-4-YL)-L-ALANINE'>OHI</scene></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=6g1g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6g1g OCA], [http://pdbe.org/6g1g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6g1g RCSB], [http://www.ebi.ac.uk/pdbsum/6g1g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6g1g ProSAT]</span></td></tr>

</table>

== Publication Abstract from PubMed ==

The recent discovery of `lytic' polysaccharide monooxygenases, copper-dependent enzymes for biomass degradation, has provided new impetus for the analysis of unusual metal-ion sites in carbohydrate-active enzymes. In this context, the CAZY family GH124 endoglucanase from Ruminiclostridium thermocellum contains an unusual metal-ion site, which was originally modelled as a Ca(2+) site but features aspartic acid, asparagine and two histidine imidazoles as coordinating residues, which are more consistent with a transition-metal binding environment. It was sought to analyse whether the GH124 metal-ion site might accommodate other metals. It is demonstrated through thermal unfolding experiments that this metal-ion site can accommodate a range of transition metals (Fe(2+), Cu(2+), Mn(2+) and Ni(2+)), whilst the three-dimensional structure and mass spectrometry show that one of the histidines is partially covalently modified and is present as a 2-oxohistidine residue; a feature that is rarely observed but that is believed to be involved in an `off-switch' to transition-metal binding. Atomic resolution (<1.1 A) complexes define the metal-ion site and also reveal the binding of an unusual fructosylated oligosaccharide, which was presumably present as a contaminant in the cellohexaose used for crystallization. Although it has not been possible to detect a biological role for the unusual metal-ion site, this work highlights the need to study some of the many metal-ion sites in carbohydrate-active enzymes that have long been overlooked or previously mis-assigned.

~~Authors:~~ Urresti, S., Davies~~, G~~.J., ~~Walton, P~~.H.

Structural studies of the unusual metal-ion site of the GH124 endoglucanase from Ruminiclostridium thermocellum.,Urresti S, Cartmell A, Liu F, Walton PH, Davies GJ Acta Crystallogr F Struct Biol Commun. 2018 Aug 1;74(Pt 8):496-505. doi:, 10.1107/S2053230X18006842. Epub 2018 Aug 1. PMID:30084399<ref>PMID:30084399</ref>

~~Description~~: ~~GH124 cellulase from Ruminiclostridium thermocellum in complex with Mn and cellotriose~~

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

[[Category: ~~Unreleased Structures~~]]

</div>

== References ==

__TOC__

</StructureSection>

[[Category: Davies, G J]]

[[Category: Urresti, S]]

[[Category: ~~Davies~~, ~~G.J~~]]

[[Category: Walton, P H]]

[[Category: ~~Walton, P.H~~]]

[[Category: 2-oxohistidine]]

[[Category: Cellulase]]

[[Category: Hydrolase]]

[[Category: Metal binding]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6g1g is ON HOLD  until Paper Publication
+==GH124 cellulase from Ruminiclostridium thermocellum in complex with Mn and cellotriose==
+<StructureSection load='6g1g' size='340' side='right' caption='[[6g1g]], [[Resolution|resolution]] 1.04&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6g1g]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6G1G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6G1G FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
+<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=OHI:3-(2-OXO-2H-IMIDAZOL-4-YL)-L-ALANINE'>OHI</scene></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=6g1g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6g1g OCA], [http://pdbe.org/6g1g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6g1g RCSB], [http://www.ebi.ac.uk/pdbsum/6g1g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6g1g ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The recent discovery of `lytic' polysaccharide monooxygenases, copper-dependent enzymes for biomass degradation, has provided new impetus for the analysis of unusual metal-ion sites in carbohydrate-active enzymes. In this context, the CAZY family GH124 endoglucanase from Ruminiclostridium thermocellum contains an unusual metal-ion site, which was originally modelled as a Ca(2+) site but features aspartic acid, asparagine and two histidine imidazoles as coordinating residues, which are more consistent with a transition-metal binding environment. It was sought to analyse whether the GH124 metal-ion site might accommodate other metals. It is demonstrated through thermal unfolding experiments that this metal-ion site can accommodate a range of transition metals (Fe(2+), Cu(2+), Mn(2+) and Ni(2+)), whilst the three-dimensional structure and mass spectrometry show that one of the histidines is partially covalently modified and is present as a 2-oxohistidine residue; a feature that is rarely observed but that is believed to be involved in an `off-switch' to transition-metal binding. Atomic resolution (&lt;1.1 A) complexes define the metal-ion site and also reveal the binding of an unusual fructosylated oligosaccharide, which was presumably present as a contaminant in the cellohexaose used for crystallization. Although it has not been possible to detect a biological role for the unusual metal-ion site, this work highlights the need to study some of the many metal-ion sites in carbohydrate-active enzymes that have long been overlooked or previously mis-assigned.
-Authors: Urresti, S., Davies, G.J., Walton, P.H.
+Structural studies of the unusual metal-ion site of the GH124 endoglucanase from Ruminiclostridium thermocellum.,Urresti S, Cartmell A, Liu F, Walton PH, Davies GJ Acta Crystallogr F Struct Biol Commun. 2018 Aug 1;74(Pt 8):496-505. doi:, 10.1107/S2053230X18006842. Epub 2018 Aug 1. PMID:30084399<ref>PMID:30084399</ref>
-Description: GH124 cellulase from Ruminiclostridium thermocellum in complex with Mn and cellotriose
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6g1g" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Davies, G J]]
 [[Category: Urresti, S]]
-[[Category: Davies, G.J]]
+[[Category: Walton, P H]]
-[[Category: Walton, P.H]]
+[[Category: 2-oxohistidine]]
+[[Category: Cellulase]]
+[[Category: Hydrolase]]
+[[Category: Metal binding]]