1cem: Difference between revisions

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New page: left|200px<br /><applet load="1cem" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cem, resolution 1.65Å" /> '''ENDOGLUCANASE A (CEL...
 
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[[Image:1cem.jpg|left|200px]]<br /><applet load="1cem" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1cem, resolution 1.65&Aring;" />
'''ENDOGLUCANASE A (CELA) CATALYTIC CORE, RESIDUES 33-395'''<br />


==Overview==
==ENDOGLUCANASE A (CELA) CATALYTIC CORE, RESIDUES 33-395==
BACKGROUND. Cellulases, which catalyze the hydrolysis of glycosidic bonds, in cellulose, can be classified into several different protein families., Endoglucanase CelA is a member of glycosyl hydrolase family 8, a family, for which no structural information was previously available. RESULTS. The, crystal structure of CelA was determined by multiple isomorphous, replacement and refined to 1.65 A resolution. The protein folds into a, regular (alpha/alpha)6 barrel formed by six inner and six outer alpha, helices. Cello-oligosaccharides bind to an acidic cleft containing at, least five D-glucosyl-binding subsites (A-E) such that the scissile, glycosidic linkage lies between subsites C and D. The strictly conserved, residue Glu95, which occupies the center of the substrate-binding cleft, and is hydrogen bonded to the glycosidic oxygen, has been assigned the, catalytic role of proton donor. CONCLUSIONS. The present analysis provides, a basis for modeling homologous family 8 cellulases. The architecture of, the active-site cleft, presenting at least five glucosyl-binding subsites, explains why family 8 cellulases cleave cello-oligosaccharide polymers, that are at least five D-glycosyl subunits long. Furthermore, the, structure of CelA allows comparison with (alpha/alpha)6 barrel, glycosidases that are not related in sequence, suggesting a possible, albeit distant, evolutionary relationship between different families of, glycosyl hydrolases.
<StructureSection load='1cem' size='340' side='right'caption='[[1cem]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1cem]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acetivibrio_thermocellus Acetivibrio thermocellus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CEM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CEM 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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1cem FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cem OCA], [https://pdbe.org/1cem PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cem RCSB], [https://www.ebi.ac.uk/pdbsum/1cem PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cem ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GUNA_ACET2 GUNA_ACET2] 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]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ce/1cem_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=1cem ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1CEM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_thermocellum Clostridium thermocellum]. 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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CEM OCA].
*[[Glucanase 3D structures|Glucanase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
The crystal structure of endoglucanase CelA, a family 8 glycosyl hydrolase from Clostridium thermocellum., Alzari PM, Souchon H, Dominguez R, Structure. 1996 Mar 15;4(3):265-75. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8805535 8805535]
[[Category: Acetivibrio thermocellus]]
[[Category: Cellulase]]
[[Category: Large Structures]]
[[Category: Clostridium thermocellum]]
[[Category: Alzari PM]]
[[Category: Single protein]]
[[Category: Alzari, P.M.]]
[[Category: cellulase]]
[[Category: clostridium thermocellum]]
[[Category: family d/8 of glycosyl hydrolases]]
[[Category: glycosyl hydrolase]]
[[Category: glycosyltransferase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:23:28 2007''

Latest revision as of 06:42, 7 February 2024

ENDOGLUCANASE A (CELA) CATALYTIC CORE, RESIDUES 33-395

1cem, resolution 1.65Å

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