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1ocb

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Revision as of 06:36, 25 June 2020

Structure of the wild-type cellobiohydrolase Cel6A from Humicolas insolens in complex with a fluorescent substrate

Structural highlights

1ocb is a 2 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, 1ocj, 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, ProSAT

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/1ocb"

@@ Line 3: / Line 3: @@
 <StructureSection load='1ocb' size='340' side='right'caption='[[1ocb]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ocb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_16454 Atcc 16454]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OCB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OCB FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ocb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_16454 Atcc 16454]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OCB OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1OCB 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=FLG:FLUORESCEINYLTHIOUREIDO'>FLG</scene>, <scene name='pdbligand=GDA:4-DEOXY-4-AMINO-BETA-D-GLUCOSE'>GDA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=GTM:O1-METHYL-4-DEOXY-4-THIO-BETA-D-GLUCOSE'>GTM</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=FLG:FLUORESCEINYLTHIOUREIDO'>FLG</scene>, <scene name='pdbligand=GDA:4-DEOXY-4-AMINO-BETA-D-GLUCOSE'>GDA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=GTM:O1-METHYL-4-DEOXY-4-THIO-BETA-D-GLUCOSE'>GTM</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bvw|1bvw]], [[1gz1|1gz1]], [[1hgw|1hgw]], [[1hgy|1hgy]], [[1oc5|1oc5]], [[1oc6|1oc6]], [[1oc7|1oc7]], [[1ocj|1ocj]], [[1ocn|1ocn]], [[1qjw|1qjw]], [[1qk0|1qk0]], [[1qk2|1qk2]], [[2bvw|2bvw]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulose_1,4-beta-cellobiosidase_(non-reducing_end) Cellulose 1,4-beta-cellobiosidase (non-reducing end)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.91 3.2.1.91] </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=1ocb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ocb OCA], [http://pdbe.org/1ocb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ocb RCSB], [http://www.ebi.ac.uk/pdbsum/1ocb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ocb ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1ocb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ocb OCA], [http://pdbe.org/1ocb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ocb RCSB], [http://www.ebi.ac.uk/pdbsum/1ocb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ocb ProSAT]</span></td></tr>
 </table>
 == Evolutionary Conservation ==

1ocb

From Proteopedia

Revision as of 06:36, 25 June 2020

Structure of the wild-type cellobiohydrolase Cel6A from Humicolas insolens in complex with a fluorescent substrate

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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