1fae

<table><tr><td colspan='2'>[[1fae]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_35319 Atcc 35319]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FAE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FAE FirstGlance]. <br>

</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></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1fce|1fce]], [[1f9d|1f9d]], [[1f9o|1f9o]], [[1fbo|1fbo]], [[1fbw|1fbw]]</div></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] </span></td></tr>

[[https://www.uniprot.org/uniprot/GUNF_CLOCE GUNF_CLOCE]] Probable endoglucanase involved in the degradation of cellulose or related beta-glucans.

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== Publication Abstract from PubMed ==

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.

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:10985769<ref>PMID:10985769</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1fae" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Atcc 35319]]

[[Category: Cellulase]]

[[Category: Belaich, J P]]

[[Category: Driguez, H]]

[[Category: Haser, R]]

[[Category: Parsiegla, G]]

[[Category: Reverbel-Leroy, C]]

[[Category: Tardif, C]]

[[Category: Protein-cellobiose complex]]