1e8q

<StructureSection load='1e8q' size='340' side='right'caption='[[1e8q]], [[NMR_Ensembles_of_Models | 5 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1e8q]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pireq Pireq]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E8Q OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1E8Q FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1e8p|1e8p]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cel45A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=99929 PIREQ])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1e8q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e8q OCA], [http://pdbe.org/1e8q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e8q RCSB], [http://www.ebi.ac.uk/pdbsum/1e8q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1e8q ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

The recycling of photosynthetically fixed carbon in plant cell walls is a key microbial process. In anaerobes, the degradation is carried out by a high molecular weight multifunctional complex termed the cellulosome. This consists of a number of independent enzyme components, each of which contains a conserved dockerin domain, which functions to bind the enzyme to a cohesin domain within the protein scaffoldin protein. Here we describe the first three-dimensional structure of a fungal dockerin, the N-terminal dockerin of Cel45A from the anaerobic fungus Piromyces equi. The structure contains a novel fold of 42 residues. The ligand binding site consists of residues Trp 35, Tyr 8 and Asp 23, which are conserved in all fungal dockerins. The binding site is on the opposite side of the N- and C-termini of the molecule, implying that tandem dockerin domains, seen in the majority of anaerobic fungal plant cell wall degrading enzymes, could present multiple simultaneous binding sites and, therefore, permit tailoring of binding to catalytic demands.

Characterization of a cellulosome dockerin domain from the anaerobic fungus Piromyces equi.,Raghothama S, Eberhardt RY, Simpson P, Wigelsworth D, White P, Hazlewood GP, Nagy T, Gilbert HJ, Williamson MP Nat Struct Biol. 2001 Sep;8(9):775-8. PMID:11524680<ref>PMID:11524680</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 1e8q" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Pireq]]

[[Category: Eberhardt, R Y]]

[[Category: Gilbert, H J]]

[[Category: Hazlewood, G P]]

[[Category: Raghothama, S]]

[[Category: Simpson, P J]]

[[Category: White, P]]

[[Category: Williamson, M P]]

[[Category: Cellulose docking domain]]