1j84

<table><tr><td colspan='2'>[[1j84]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_35296 Atcc 35296]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J84 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1J84 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1j83|1j83]]</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1j84 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j84 OCA], [http://pdbe.org/1j84 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1j84 RCSB], [http://www.ebi.ac.uk/pdbsum/1j84 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1j84 ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

The crystal structure of the Clostridium cellulovorans carbohydrate-binding module (CBM) belonging to family 17 has been solved to 1.7 A resolution by multiple anomalous dispersion methods. CBM17 binds to non-crystalline cellulose and soluble beta-1,4-glucans, with a minimal binding requirement of cellotriose and optimal affinity for cellohexaose. The crystal structure of CBM17 complexed with cellotetraose solved at 2.0 A resolution revealed that binding occurs in a cleft on the surface of the molecule involving two tryptophan residues and several charged amino acids. Thermodynamic binding studies and alanine scanning mutagenesis in combination with the cellotetraose complex structure allowed the mapping of the CBM17 binding cleft. In contrast to the binding groove characteristic of family 4 CBMs, family 17 CBMs appear to have a very shallow binding cleft that may be more accessible to cellulose chains in non-crystalline cellulose than the deeper binding clefts of family 4 CBMs. The structural differences in these two modules may reflect non-overlapping binding niches on cellulose surfaces.

Recognition of cello-oligosaccharides by a family 17 carbohydrate-binding module: an X-ray crystallographic, thermodynamic and mutagenic study.,Notenboom V, Boraston AB, Chiu P, Freelove AC, Kilburn DG, Rose DR J Mol Biol. 2001 Dec 7;314(4):797-806. PMID:11733998<ref>PMID:11733998</ref>

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

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== References ==

<references/>

[[Category: Atcc 35296]]

[[Category: Cellulase]]

[[Category: Boraston, A B]]

[[Category: Chiu, P]]

[[Category: Freelove, A C.J]]

[[Category: Kilburn, D G]]

[[Category: Notenboom, V]]

[[Category: Rose, D R]]

[[Category: Hydrolase]]