1exp

From Proteopedia

(Difference between revisions)

Current revision

BETA-1,4-GLYCANASE CEX-CD

Structural highlights

1exp is a 1 chain structure with sequence from Cellulomonas fimi. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.8Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GUX_CELFI Hydrolyzes both cellulose and xylan. Has also weak endoglucanase activity. The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.

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 three-dimensional structure of a catalytically competent glycosyl-enzyme intermediate of a retaining beta-1,4-glycanase has been determined at a resolution of 1.8 A by X-ray diffraction. A fluorinated slow substrate forms an alpha-D-glycopyranosyl linkage to one of the two invariant carboxylates, Glu 233, as supported in solution by 19F-NMR studies. The resulting ester linkage is coplanar with the cyclic oxygen of the proximal saccharide and is inferred to form a strong hydrogen bond with the 2-hydroxyl of that saccharide unit in natural substrates. The active-site architecture of this covalent intermediate gives insights into both the classical double-displacement catalytic mechanism and the basis for the enzyme's specificity.

Crystallographic observation of a covalent catalytic intermediate in a beta-glycosidase.,White A, Tull D, Johns K, Withers SG, Rose DR Nat Struct Biol. 1996 Feb;3(2):149-54. PMID:8564541^[1]

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

References

↑ White A, Tull D, Johns K, Withers SG, Rose DR. Crystallographic observation of a covalent catalytic intermediate in a beta-glycosidase. Nat Struct Biol. 1996 Feb;3(2):149-54. PMID:8564541

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 3: / Line 3: @@
 <StructureSection load='1exp' size='340' side='right'caption='[[1exp]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1exp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacterium_fimi"_mcbeth_and_scales_1913 "bacterium fimi" mcbeth and scales 1913]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EXP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EXP FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1exp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cellulomonas_fimi Cellulomonas fimi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EXP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EXP 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>, <scene name='pdbligand=G2F:2-DEOXY-2-FLUORO-ALPHA-D-GLUCOPYRANOSE'>G2F</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</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=G2F:2-DEOXY-2-FLUORO-ALPHA-D-GLUCOPYRANOSE'>G2F</scene>, <scene name='pdbligand=PRD_900050:2-deoxy-2-fluoro-beta-cellobiose'>PRD_900050</scene></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=1exp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1exp OCA], [https://pdbe.org/1exp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1exp RCSB], [https://www.ebi.ac.uk/pdbsum/1exp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1exp ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/GUX_CELFI GUX_CELFI] Hydrolyzes both cellulose and xylan. Has also weak endoglucanase activity.  The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 12: / Line 15: @@
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ex/1exp_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 30: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Bacterium fimi mcbeth and scales 1913]]
+[[Category: Cellulomonas fimi]]
 [[Category: Large Structures]]
-[[Category: Johns, K L]]
+[[Category: Johns KL]]
-[[Category: Rose, D R]]
+[[Category: Rose DR]]
-[[Category: Tull, D]]
+[[Category: Tull D]]
-[[Category: White, A]]
+[[Category: White A]]
-[[Category: Withers, S G]]
+[[Category: Withers SG]]
-[[Category: Cellulose degradation]]
-[[Category: Glycosidase]]
-[[Category: Hydrolase]]

1exp

From Proteopedia

Current revision

BETA-1,4-GLYCANASE CEX-CD

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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