1kwf

From Proteopedia

(Difference between revisions)

Revision as of 14:44, 27 October 2021

Atomic Resolution Structure of an Inverting Glycosidase in Complex with Substrate

Structural highlights

1kwf is a 1 chain structure with sequence from "ruminiclostridium_thermocellum"_(viljoen_et_al._1926)_yutin_and_galperin_2013 "ruminiclostridium thermocellum" (viljoen et al. 1926) yutin and galperin 2013. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1cem
Gene:	celA ("Ruminiclostridium thermocellum" (Viljoen et al. 1926) Yutin and Galperin 2013)
Activity:	Cellulase, with EC number 3.2.1.4
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[GUNA_CLOTM] This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-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

The crystal structure of Clostridium thermocellum endoglucanase CelA in complex with cellopentaose has been determined at 0.94 A resolution. The oligosaccharide occupies six D-glucosyl-binding subsites, three on either side of the scissile glycosidic linkage. The substrate and product of the reaction occupy different positions at the reducing end of the cleft, where an extended array of hydrogen-bonding interactions with water molecules fosters the departure of the leaving group. Severe torsional strain upon the bound substrate forces a distorted boat(2,5) B conformation for the glucosyl residue bound at subsite -1, which facilitates the formation of an oxocarbenium ion intermediate and might favor the breakage of the sugar ring concomitant with catalysis.

Atomic (0.94 A) resolution structure of an inverting glycosidase in complex with substrate.,Guerin DM, Lascombe MB, Costabel M, Souchon H, Lamzin V, Beguin P, Alzari PM J Mol Biol. 2002 Mar 8;316(5):1061-9. PMID:11884144^[1]

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

References

↑ Guerin DM, Lascombe MB, Costabel M, Souchon H, Lamzin V, Beguin P, Alzari PM. Atomic (0.94 A) resolution structure of an inverting glycosidase in complex with substrate. J Mol Biol. 2002 Mar 8;316(5):1061-9. PMID:11884144 doi:10.1006/jmbi.2001.5404

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/1kwf"

@@ Line 3: / Line 3: @@
 <StructureSection load='1kwf' size='340' side='right'caption='[[1kwf]], [[Resolution|resolution]] 0.94&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1kwf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"ruminiclostridium_thermocellum"_(viljoen_et_al._1926)_yutin_and_galperin_2013 "ruminiclostridium thermocellum" (viljoen et al. 1926) yutin and galperin 2013]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KWF OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1KWF FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1kwf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"ruminiclostridium_thermocellum"_(viljoen_et_al._1926)_yutin_and_galperin_2013 "ruminiclostridium thermocellum" (viljoen et al. 1926) yutin and galperin 2013]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KWF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KWF FirstGlance]. <br>
 </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></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1cem|1cem]]</div></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">celA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1515 "Ruminiclostridium thermocellum" (Viljoen et al. 1926) Yutin and Galperin 2013])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">celA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1515 "Ruminiclostridium thermocellum" (Viljoen et al. 1926) Yutin and Galperin 2013])</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [https://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://proteopedia.org/fgij/fg.htm?mol=1kwf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kwf OCA], [http://pdbe.org/1kwf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kwf RCSB], [http://www.ebi.ac.uk/pdbsum/1kwf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kwf ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kwf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kwf OCA], [https://pdbe.org/1kwf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kwf RCSB], [https://www.ebi.ac.uk/pdbsum/1kwf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kwf ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/GUNA_CLOTM GUNA_CLOTM]] This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
+[[https://www.uniprot.org/uniprot/GUNA_CLOTM GUNA_CLOTM]] This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1kwf

From Proteopedia

Revision as of 14:44, 27 October 2021

Atomic Resolution Structure of an Inverting Glycosidase in Complex with Substrate

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