1oc6

From Proteopedia

(Difference between revisions)

Revision as of 07:03, 7 February 2018

structure native of the D405N mutant of the CELLOBIOHYDROLASE CEL6A FROM HUMICOLA INSOLENS at 1.5 angstrom resolution

Structural highlights

1oc6 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, 1oc7, 1ocb, 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 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1oc6"

@@ Line 1: / Line 1: @@
-==STRUCTURE NATIVE OF THE D405N MUTANT OF THE CELLOBIOHYDROLASE CEL6A FROM HUMICOLA INSOLENS AT 1.5 ANGSTROM RESOLUTION==
+==structure native of the D405N mutant of the CELLOBIOHYDROLASE CEL6A FROM HUMICOLA INSOLENS at 1.5 angstrom resolution==
 <StructureSection load='1oc6' size='340' side='right' caption='[[1oc6]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
 == Structural highlights ==
@@ Line 6: / Line 7: @@
 <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]], [[1oc7|1oc7]], [[1ocb|1ocb]], [[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=1oc6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oc6 OCA], [http://pdbe.org/1oc6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1oc6 RCSB], [http://www.ebi.ac.uk/pdbsum/1oc6 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=1oc6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oc6 OCA], [http://pdbe.org/1oc6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1oc6 RCSB], [http://www.ebi.ac.uk/pdbsum/1oc6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1oc6 ProSAT]</span></td></tr>
 </table>
 == Evolutionary Conservation ==
@@ Line 12: / Line 13: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oc/1oc6_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oc/1oc6_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 27: / Line 28: @@
 </div>
 <div class="pdbe-citations 1oc6" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Cellobiohydrolase|Cellobiohydrolase]]
 == References ==
 <references/>

1oc6

From Proteopedia

Revision as of 07:03, 7 February 2018

structure native of the D405N mutant of the CELLOBIOHYDROLASE CEL6A FROM HUMICOLA INSOLENS at 1.5 angstrom resolution

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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