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1ocj

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Revision as of 04:16, 8 February 2016

Mutant D416A of the CELLOBIOHYDROLASE CEL6A FROM HUMICOLA INSOLENS in complex with a THIOPENTASACCHARIDE at 1.3 angstrom resolution

Structural highlights

1ocj is a 1 chain structure with sequence from Atcc 16454. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , , , ,
Related:	1bvw, 1gz1, 1hgw, 1hgy, 1oc5, 1oc6, 1oc7, 1ocb, 1ocn, 1qjw, 1qk0, 1qk2, 2bvw
Activity:	Cellulose 1,4-beta-cellobiosidase (non-reducing end), with EC number 3.2.1.91
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

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

The enzymatic digestion of cellulose entails intimate involvement of cellobiohydrolases, whose characteristic active-center tunnel contributes to a processive degradation of the polysaccharide. The cellobiohydrolase Cel6A displays an active site within a tunnel formed by two extended loops, which are known to open and close in response to ligand binding. Here we present five structures of wild-type and mutant forms of Cel6A from Humicola insolens in complex with nonhydrolyzable thio-oligosaccharides, at resolutions from 1.7-1.1 A, dissecting the structural accommodation of a processing substrate chain through the active center during hydrolysis. Movement of ligand is facilitated by extensive solvent-mediated interactions and through flexibility in the hydrophobic surfaces provided by a sheath of tryptophan residues.

Structural basis for ligand binding and processivity in cellobiohydrolase Cel6A from Humicola insolens.,Varrot A, Frandsen TP, von Ossowski I, Boyer V, Cottaz S, Driguez H, Schulein M, Davies GJ Structure. 2003 Jul;11(7):855-64. PMID:12842048^[1]

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

References

↑ Varrot A, Frandsen TP, von Ossowski I, Boyer V, Cottaz S, Driguez H, Schulein M, Davies GJ. Structural basis for ligand binding and processivity in cellobiohydrolase Cel6A from Humicola insolens. Structure. 2003 Jul;11(7):855-64. PMID:12842048

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ocj"

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     <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=1ocj ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">

1ocj

From Proteopedia

Revision as of 04:16, 8 February 2016

Mutant D416A of the CELLOBIOHYDROLASE CEL6A FROM HUMICOLA INSOLENS in complex with a THIOPENTASACCHARIDE at 1.3 angstrom resolution

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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