1daq

<StructureSection load='1daq' size='340' side='right'caption='[[1daq]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1daq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"ruminiclostridium_thermocellum"_(viljoen_et_al._1926)_yutin_and_galperin_2013 "ruminiclostridium thermocellum" (viljoen et al. 1926) yutin and galperin 2013]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DAQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DAQ 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></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1dav|1dav]]</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/GUNS_CLOTM GUNS_CLOTM]] This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

The type I dockerin domain is responsible for incorporating its associated glycosyl hydrolase into the bacterial cellulosome, a multienzyme cellulolytic complex, via its interaction with a receptor domain (cohesin domain) of the cellulosomal scaffolding subunit. The highly conserved dockerin domain is characterized by two Ca(2+)-binding sites with sequence similarity to the EF-hand motif. Here, we present the three-dimensional solution structure of the 69 residue dockerin domain of Clostridium thermocellum cellobiohydrolase CelS. Torsion angle dynamics calculations utilizing a total of 728 NOE-derived distance constraints and 79 torsion angle restraints yielded an ensemble of 20 structures with an average backbone r.m.s.d. for residues 5 to 29 and 32 to 66 of 0.54 A from the mean structure. The structure consists of two Ca(2+)-binding loop-helix motifs connected by a linker; the E helices entering each loop of the classical EF-hand motif are absent from the dockerin domain. Each dockerin Ca(2+)-binding subdomain is stabilized by a cluster of buried hydrophobic side-chains. Structural comparisons reveal that, in its non-complexed state, the dockerin fold displays a dramatic departure from that of Ca(2+)-bound EF-hand domains. A putative cohesin-binding surface, comprised of conserved hydrophobic and basic residues, is proposed, providing new insight into cellulosome assembly.

Solution structure of a type I dockerin domain, a novel prokaryotic, extracellular calcium-binding domain.,Lytle BL, Volkman BF, Westler WM, Heckman MP, Wu JH J Mol Biol. 2001 Mar 30;307(3):745-53. PMID:11273698<ref>PMID:11273698</ref>

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

</div>

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

[[Category: Cellulase]]

[[Category: Heckman, M P]]

[[Category: Lytle, B L]]

[[Category: Volkman, B F]]

[[Category: Westler, W M]]

[[Category: Wu, J H.D]]

[[Category: Hydrolase]]