1g9g
From Proteopedia
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|PDB= 1g9g |SIZE=350|CAPTION= <scene name='initialview01'>1g9g</scene>, resolution 1.90Å | |PDB= 1g9g |SIZE=350|CAPTION= <scene name='initialview01'>1g9g</scene>, resolution 1.90Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/ | + | |ACTIVITY= <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> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1g9j|1G9J]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g9g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g9g OCA], [http://www.ebi.ac.uk/pdbsum/1g9g PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1g9g RCSB]</span> | ||
}} | }} | ||
| Line 20: | Line 23: | ||
==Reference== | ==Reference== | ||
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:[http://www.ncbi.nlm.nih.gov/pubmed/18035374 18035374] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/18035374 18035374] | ||
| + | [[Category: Cellulase]] | ||
[[Category: Clostridium cellulolyticum]] | [[Category: Clostridium cellulolyticum]] | ||
| - | [[Category: Hydrolase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Belaich, J P.]] | [[Category: Belaich, J P.]] | ||
| Line 28: | Line 31: | ||
[[Category: Parsiegla, G.]] | [[Category: Parsiegla, G.]] | ||
[[Category: Tardif, C.]] | [[Category: Tardif, C.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: MG]] | ||
[[Category: cellulase]] | [[Category: cellulase]] | ||
[[Category: processive-endo]] | [[Category: processive-endo]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:39:31 2008'' |
Revision as of 17:39, 30 March 2008
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| , resolution 1.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Cellulase, with EC number 3.2.1.4 | ||||||
| Related: | 1G9J
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
XTAL-STRUCTURE OF THE FREE NATIVE CELLULASE CEL48F
Overview
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.
About this Structure
1G9G is a Single protein structure of sequence from Clostridium cellulolyticum. Full crystallographic information is available from OCA.
Reference
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
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