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[[Image:4a3h.gif|left|200px]]
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{{STRUCTURE_4a3h|  PDB=4a3h  |  SCENE=  }}
'''2',4' DINITROPHENYL-2-DEOXY-2-FLURO-B-D-CELLOBIOSIDE COMPLEX OF THE ENDOGLUCANASE CEL5A FROM BACILLUS AGARADHAERENS AT 1.6 A RESOLUTION'''


==2',4' DINITROPHENYL-2-DEOXY-2-FLURO-B-D-CELLOBIOSIDE COMPLEX OF THE ENDOGLUCANASE CEL5A FROM BACILLUS AGARADHAERENS AT 1.6 A RESOLUTION==
<StructureSection load='4a3h' size='340' side='right'caption='[[4a3h]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4a3h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Salipaludibacillus_agaradhaerens Salipaludibacillus agaradhaerens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A3H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A3H FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DCB:2,4-DINITROPHENYL-2-DEOXY-2-FLUORO-BETA-D-CELLOBIOSIDE'>DCB</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=4a3h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a3h OCA], [https://pdbe.org/4a3h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a3h RCSB], [https://www.ebi.ac.uk/pdbsum/4a3h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a3h ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GUN5_SALAG GUN5_SALAG]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a3/4a3h_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <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/main_output.php?pdb_ID=4a3h ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The enzymatic hydrolysis of O-glycosidic linkages is one of the most diverse and widespread reactions in nature and involves a classic "textbook" enzyme mechanism. A multidisciplinary analysis of a beta-glycoside hydrolase, the Cel5A from Bacillus agaradhaerens, is presented in which the structures of each of the native, substrate, covalent-intermediate, and product complexes have been determined and their interconversions analyzed kinetically, providing unprecedented insights into the mechanism of this enzyme class. Substrate is bound in a distorted 1S3 skew-boat conformation, thereby presenting the anomeric carbon appropriately for nucleophilic attack as well as satisfying the stereoelectronic requirements for an incipient oxocarbenium ion. Leaving group departure results in the trapping of a covalent alpha-glycosyl-enzyme intermediate in which the sugar adopts an undistorted 4C1 conformation. Finally, hydrolysis of this intermediate yields a product complex in which the sugar is bound in a partially disordered mode, consistent with unfavorable interactions and low product affinity.


==Overview==
Snapshots along an enzymatic reaction coordinate: analysis of a retaining beta-glycoside hydrolase.,Davies GJ, Mackenzie L, Varrot A, Dauter M, Brzozowski AM, Schulein M, Withers SG Biochemistry. 1998 Aug 25;37(34):11707-13. PMID:9718293<ref>PMID:9718293</ref>
The enzymatic hydrolysis of O-glycosidic linkages is one of the most diverse and widespread reactions in nature and involves a classic "textbook" enzyme mechanism. A multidisciplinary analysis of a beta-glycoside hydrolase, the Cel5A from Bacillus agaradhaerens, is presented in which the structures of each of the native, substrate, covalent-intermediate, and product complexes have been determined and their interconversions analyzed kinetically, providing unprecedented insights into the mechanism of this enzyme class. Substrate is bound in a distorted 1S3 skew-boat conformation, thereby presenting the anomeric carbon appropriately for nucleophilic attack as well as satisfying the stereoelectronic requirements for an incipient oxocarbenium ion. Leaving group departure results in the trapping of a covalent alpha-glycosyl-enzyme intermediate in which the sugar adopts an undistorted 4C1 conformation. Finally, hydrolysis of this intermediate yields a product complex in which the sugar is bound in a partially disordered mode, consistent with unfavorable interactions and low product affinity.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
4A3H is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_agaradhaerens Bacillus agaradhaerens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A3H OCA].
</div>
<div class="pdbe-citations 4a3h" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Snapshots along an enzymatic reaction coordinate: analysis of a retaining beta-glycoside hydrolase., Davies GJ, Mackenzie L, Varrot A, Dauter M, Brzozowski AM, Schulein M, Withers SG, Biochemistry. 1998 Aug 25;37(34):11707-13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9718293 9718293]
*[[Glucanase 3D structures|Glucanase 3D structures]]
[[Category: Bacillus agaradhaerens]]
== References ==
[[Category: Cellulase]]
<references/>
[[Category: Single protein]]
__TOC__
[[Category: Andersen, K.]]
</StructureSection>
[[Category: Brzozowski, A M.]]
[[Category: Large Structures]]
[[Category: Davies, G J.]]
[[Category: Salipaludibacillus agaradhaerens]]
[[Category: Mackenzie, L.]]
[[Category: Andersen K]]
[[Category: Schulein, M.]]
[[Category: Brzozowski AM]]
[[Category: Withers, S G.]]
[[Category: Davies GJ]]
[[Category: Cellulose degradation]]
[[Category: Mackenzie L]]
[[Category: Distortion]]
[[Category: Schulein M]]
[[Category: Endoglucanase]]
[[Category: Withers SG]]
[[Category: Glycoside hydrolase family 5]]
[[Category: Hydrolase]]
[[Category: Michaelis complex. skew-boat]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 22:20:19 2008''

Latest revision as of 00:35, 28 December 2023

2',4' DINITROPHENYL-2-DEOXY-2-FLURO-B-D-CELLOBIOSIDE COMPLEX OF THE ENDOGLUCANASE CEL5A FROM BACILLUS AGARADHAERENS AT 1.6 A RESOLUTION

4a3h, resolution 1.65Å

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