1a3h

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[[Image:1a3h.gif|left|200px]]<br />
 
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<applet load="1a3h" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1a3h, resolution 1.57&Aring;" />
 
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'''ENDOGLUCANASE CEL5A FROM BACILLUS AGARADHERANS AT 1.6A RESOLUTION'''<br />
 
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==Overview==
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==ENDOGLUCANASE CEL5A FROM BACILLUS AGARADHERANS AT 1.6A RESOLUTION==
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The enzymatic degradation of cellulose, by cellulases, is not only, industrially important in the food, paper, and textile industries but also, a potentially useful method for the environmentally friendly recycling of, municipal waste. An understanding of the structural and mechanistic, requirements for the hydrolysis of the beta-1,4 glycosidic bonds of, cellulose is an essential prerequisite for beneficial engineering of, cellulases for these processes. Cellulases have been classified into 13 of, the 62 glycoside hydrolase families [Henrissat, B., and Bairoch, A. (1996), Biochem J. 316, 695-696]. The structure of the catalytic core of the, family 5 endoglucanase, Ce15A, from the alkalophilic Bacillus agaradherans, has been solved by multiple isomorphous replacement at 1.6 A resolution., Ce15A has the (alpha/beta)8 barrel structure and signature structural, features typical of the grouping of glycoside hydrolase families known as, clan GH-A, with the catalytic acid/base Glu 139 and nucleophile Glu 228 on, barrel strands beta 4 and beta 7 as expected. In addition to the native, enzyme, the 2.0 A resolution structure of the cellobiose-bound form of the, enzyme has also been determined. Cellobiose binds preferentially in the -2, and -3 subsites of the enzyme. Kinetic studies on the isolated catalytic, core domain of Ce15A, using a series of reduced cellodextrins as, substrates, suggest approximately five to six binding sites, consistent, with the shape and size of the cleft observed by crystallography.
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<StructureSection load='1a3h' size='340' side='right'caption='[[1a3h]], [[Resolution|resolution]] 1.57&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1a3h]] 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=1A3H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A3H FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.57&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1a3h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a3h OCA], [https://pdbe.org/1a3h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a3h RCSB], [https://www.ebi.ac.uk/pdbsum/1a3h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a3h ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GUN5_SALAG GUN5_SALAG]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a3/1a3h_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1a3h ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1A3H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_agaradhaerens Bacillus agaradhaerens]. Active as [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] Structure known Active Site: AVE. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1A3H OCA].
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*[[Glucanase 3D structures|Glucanase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Structure of the Bacillus agaradherans family 5 endoglucanase at 1.6 A and its cellobiose complex at 2.0 A resolution., Davies GJ, Dauter M, Brzozowski AM, Bjornvad ME, Andersen KV, Schulein M, Biochemistry. 1998 Feb 17;37(7):1926-32. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9485319 9485319]
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[[Category: Large Structures]]
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[[Category: Bacillus agaradhaerens]]
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[[Category: Salipaludibacillus agaradhaerens]]
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[[Category: Cellulase]]
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[[Category: Andersen K]]
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[[Category: Single protein]]
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[[Category: Brzozowski AM]]
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[[Category: Andersen, K.]]
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[[Category: Davies GJ]]
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[[Category: Brzozowski, A.M.]]
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[[Category: Schulein M]]
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[[Category: Davies, G.J.]]
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[[Category: Schulein, M.]]
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[[Category: cellulose degradation]]
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[[Category: endoglucanase]]
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[[Category: glycoside hydrolase family 5]]
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[[Category: hydrolase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 15:44:10 2007''
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Current revision

ENDOGLUCANASE CEL5A FROM BACILLUS AGARADHERANS AT 1.6A RESOLUTION

PDB ID 1a3h

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