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.

2qno

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 11:30, 5 September 2018

Crystal Structure of the Mutant E55Q of the Cellulase CEL48F in Complex with a Thio-Oligosaccharide

Structural highlights

2qno is a 1 chain structure with sequence from Atcc 35319. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	1g9g, 1g9j
Gene:	celCCF (ATCC 35319)
Activity:	Cellulase, with EC number 3.2.1.4
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[GUNF_CLOCE] Probable endoglucanase involved in the degradation of cellulose or related beta-glucans.

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

An efficient breakdown of lignocellulosic biomass is a prerequisite for the production of second-generation biofuels. Cellulases are key enzymes in this process. We crystallized complexes between hemithio-cello-deca and dodecaoses and the inactive mutants E44Q and E55Q of the endo-processive cellulase Cel48F, one of the most abundant cellulases in cellulosomes from Clostridium cellulolyticum, to elucidate its processive mechanism. In both complexes, the cellooligosaccharides occupy similar positions in the tunnel part of the active site but are more or less buried into the cleft, which hosts the active site. In the E44Q complex, it proceeds along the upper part of the cavity, while it occupies in the E55Q complex the same productive binding subsites in the lower part of the cavity that have previously been reported in Cel48F/cellooligosaccharide complexes. In both cases, the sugar moieties are stabilized by stacking interactions with aromatic side chains and H bonds. The upper pathway is gated by Tyr403, which blocks its access in the E55Q complex and offers a new stacking interaction in the E44Q complex. The new structural data give rise to the hypothesis of a two-step mechanism in which processive action and chain disruption occupy different subsites at the end of their trajectory. In the first part of the mechanism, the chain may smoothly slide up to the leaving group site along the upper pathway, while in the second part, the chain is cleaved in the already described productive binding position located in the lower pathway. The solved native structure of Cel48F without any bound sugar in the active site confirms the two side-chain orientations of the proton donor Glu55 as observed in the complex structures.

Structures of mutants of cellulase Cel48F of Clostridium cellulolyticum in complex with long hemithiocellooligosaccharides give rise to a new view of the substrate pathway during processive action.,Parsiegla G, Reverbel C, Tardif C, Driguez H, Haser R J Mol Biol. 2008 Jan 11;375(2):499-510. Epub 2007 Oct 22. PMID:18035374^[1]

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

References

↑ Parsiegla G, Reverbel C, Tardif C, Driguez H, Haser R. Structures of mutants of cellulase Cel48F of Clostridium cellulolyticum in complex with long hemithiocellooligosaccharides give rise to a new view of the substrate pathway during processive action. J Mol Biol. 2008 Jan 11;375(2):499-510. Epub 2007 Oct 22. PMID:18035374 doi:10.1016/j.jmb.2007.10.039

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
 ==Crystal Structure of the Mutant E55Q of the Cellulase CEL48F in Complex with a Thio-Oligosaccharide==
 <StructureSection load='2qno' size='340' side='right' caption='[[2qno]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
@@ Line 7: / Line 8: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">celCCF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1521 ATCC 35319])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] </span></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=2qno FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qno OCA], [http://pdbe.org/2qno PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2qno RCSB], [http://www.ebi.ac.uk/pdbsum/2qno PDBsum]</span></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=2qno FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qno OCA], [http://pdbe.org/2qno PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2qno RCSB], [http://www.ebi.ac.uk/pdbsum/2qno PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2qno ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 15: / Line 16: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qn/2qno_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qn/2qno_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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=2qno ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">

2qno

From Proteopedia

Revision as of 11:30, 5 September 2018

Crystal Structure of the Mutant E55Q of the Cellulase CEL48F in Complex with a Thio-Oligosaccharide

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox