1e8r

<StructureSection load='1e8r' size='340' side='right' caption='[[1e8r]], [[NMR_Ensembles_of_Models | 5 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1e8r]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_fluorescens_liquefaciens"_flugge_1886 "bacillus fluorescens liquefaciens" flugge 1886]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1ct7 1ct7]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E8R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E8R FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1clx|1clx]], [[1ct7|1ct7]], [[1qld|1qld]]</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Endo-1,4-beta-xylanase Endo-1,4-beta-xylanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.8 3.2.1.8] </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=1e8r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e8r OCA], [http://pdbe.org/1e8r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e8r RCSB], [http://www.ebi.ac.uk/pdbsum/1e8r PDBsum]</span></td></tr>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e8/1e8r_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

Plant cell wall hydrolases generally have a modular structure consisting of a catalytic domain linked to one or more noncatalytic carbohydrate-binding modules (CBMs), whose common function is to attach the enzyme to the polymeric substrate. Xylanase A from Pseudomonas fluorescens subsp. cellulosa (Pf Xyn10A) consists of a family 10 catalytic domain, an N-terminal family IIa cellulose-binding module, and an internal family 10 cellulose-binding module. The structure of the 45-residue family 10 CBM has been determined in solution using NMR. It consists of two antiparallel beta-sheets, one with two strands and one with three, with a short alpha-helix across one face of the three-stranded sheet. There is a high density of aromatic residues on one side of the protein, including three aromatic residues (Tyr8, Trp22, and Trp24), which are exposed and form a flat surface on one face, in a classical polysaccharide-binding arrangement. The fold is closely similar to that of the oligonucleotide/oligosaccharide-binding (OB) fold, but appears to have arisen by convergent evolution, because there is no sequence similarity, and the presumed binding sites are on different faces.

Solution structure of the CBM10 cellulose binding module from Pseudomonas xylanase A.,Raghothama S, Simpson PJ, Szabo L, Nagy T, Gilbert HJ, Williamson MP Biochemistry. 2000 Feb 8;39(5):978-84. PMID:10653641<ref>PMID:10653641</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 1e8r" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Bacillus fluorescens liquefaciens flugge 1886]]

[[Category: Endo-1,4-beta-xylanase]]

[[Category: Gilbert, H J]]

[[Category: Raghothama, S]]

[[Category: Simpson, P J]]

[[Category: Williamson, M P]]

[[Category: Hydrolase]]