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[[Image:1f9d.jpg|left|200px]]<br /><applet load="1f9d" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1f9d, resolution 2.3&Aring;" />
'''Crystal structure of the cellulase CEL48F from C. cellulolyticum in complex with cellotetraose'''<br />


==Overview==
==Crystal structure of the cellulase CEL48F from C. cellulolyticum in complex with cellotetraose==
Cellulase Cel48F from Clostridium cellulolyticum was described as a processive endo-cellulase. The active site is composed of a 25 A long tunnel which is followed by an open cleft. During the processive action, the cellulose substrate has to slide through the tunnel to continuously supply the leaving group site with sugar residues after the catalytic cleavage. To study this processive action in the tunnel, the native catalytic module of Cel48F and the inactive mutant E55Q, have been cocrystallized with cellobiitol, two thio-oligosaccharide inhibitors (PIPS-IG3 and IG4) and the cello-oligosaccharides cellobiose, -tetraose and -hexaose. Seven sub-sites in the tunnel section of the active center could be identified and three of the four previously reported sub-sites in the open cleft section were reconfirmed. The sub-sites observed for the thio-oligosaccharide inhibitors and oligosaccharides, respectively, were located at two different positions in the tunnel corresponding to a shift in the chain direction of about a half sugar subunit. These two positions have different patterns of stacking interactions with aromatic residues present in the tunnel. Multiple patterns are not observed in nonprocessive endo-cellulases, where only one sugar position is favored by aromatic stacking. It is therefore proposed that the aromatic residues serve as lubricating agents to reduce the sliding barrier in the processive action.
<StructureSection load='1f9d' size='340' side='right'caption='[[1f9d]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1f9d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ruminiclostridium_cellulolyticum Ruminiclostridium cellulolyticum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F9D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F9D 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]] 2.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900010:alpha-maltotetraose'>PRD_900010</scene>, <scene name='pdbligand=PRD_900030:alpha-maltopentaose'>PRD_900030</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=1f9d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f9d OCA], [https://pdbe.org/1f9d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f9d RCSB], [https://www.ebi.ac.uk/pdbsum/1f9d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f9d ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GUNF_RUMCH GUNF_RUMCH] Probable endoglucanase involved in the degradation of cellulose or related beta-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/f9/1f9d_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=1f9d ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1F9D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_cellulolyticum Clostridium cellulolyticum] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1F9D OCA].
*[[Glucanase 3D structures|Glucanase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Crystal structures of the cellulase Cel48F in complex with inhibitors and substrates give insights into its processive action., Parsiegla G, Reverbel-Leroy C, Tardif C, Belaich JP, Driguez H, Haser R, Biochemistry. 2000 Sep 19;39(37):11238-46. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10985769 10985769]
[[Category: Large Structures]]
[[Category: Cellulase]]
[[Category: Ruminiclostridium cellulolyticum]]
[[Category: Clostridium cellulolyticum]]
[[Category: Belaich JP]]
[[Category: Single protein]]
[[Category: Driguez H]]
[[Category: Belaich, J P.]]
[[Category: Haser R]]
[[Category: Driguez, H.]]
[[Category: Parsiegla G]]
[[Category: Haser, R.]]
[[Category: Reverbel-Leroy C]]
[[Category: Parsiegla, G.]]
[[Category: Tardif C]]
[[Category: Reverbel-Leroy, C.]]
[[Category: Tardif, C.]]
[[Category: CA]]
[[Category: cellulase]]
[[Category: protein-cellotetraose complex]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:36:17 2008''

Latest revision as of 07:12, 7 February 2024

Crystal structure of the cellulase CEL48F from C. cellulolyticum in complex with cellotetraose

1f9d, resolution 2.30Å

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