2c4x: Difference between revisions

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-{{Seed}}
-[[Image:2c4x.png|left|200px]]
-<!--
+==Structural basis for the promiscuous specificity of the carbohydrate- binding modules from the beta-sandwich super family==
-The line below this paragraph, containing "STRUCTURE_2c4x", creates the "Structure Box" on the page.
+<StructureSection load='2c4x' size='340' side='right'caption='[[2c4x]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2c4x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acetivibrio_thermocellus Acetivibrio thermocellus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C4X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C4X FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-{{STRUCTURE_2c4x|  PDB=2c4x  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2c4x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c4x OCA], [https://pdbe.org/2c4x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c4x RCSB], [https://www.ebi.ac.uk/pdbsum/2c4x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c4x ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/P71140_ACETH P71140_ACETH]
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c4/2c4x_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2c4x ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Enzyme systems that attack the plant cell wall contain noncatalytic carbohydrate-binding modules (CBMs) that mediate attachment to this composite structure and play a pivotal role in maximizing the hydrolytic process. Although xyloglucan, which includes a backbone of beta-1,4-glucan decorated primarily with xylose residues, is a key component of the plant cell wall, CBMs that bind to this polymer have not been identified. Here we showed that the C-terminal domain of the modular Clostridium thermocellum enzyme CtCel9D-Cel44A (formerly known as CelJ) comprises a novel CBM (designated CBM44) that binds with equal affinity to cellulose and xyloglucan. We also showed that accommodation of xyloglucan side chains is a general feature of CBMs that bind to single cellulose chains. The crystal structures of CBM44 and the other CBM (CBM30) in CtCel9D-Cel44A display a beta-sandwich fold. The concave face of both CBMs contains a hydrophobic platform comprising three tryptophan residues that can accommodate up to five glucose residues. The orientation of these aromatic residues is such that the bound ligand would adopt the twisted conformation displayed by cello-oligosaccharides in solution. Mutagenesis studies confirmed that the hydrophobic platform located on the concave face of both CBMs mediates ligand recognition. In contrast to other CBMs that bind to single polysaccharide chains, the polar residues in the binding cleft of CBM44 play only a minor role in ligand recognition. The mechanism by which these proteins are able to recognize linear and decorated beta-1,4-glucans is discussed based on the structures of CBM44 and the other CBMs that bind single cellulose chains.
-===STRUCTURAL BASIS FOR THE PROMISCUOUS SPECIFICITY OF THE CARBOHYDRATE-BINDING MODULES FROM THE BETA-SANDWICH SUPER FAMILY===
+Xyloglucan is recognized by carbohydrate-binding modules that interact with beta-glucan chains.,Najmudin S, Guerreiro CI, Carvalho AL, Prates JA, Correia MA, Alves VD, Ferreira LM, Romao MJ, Gilbert HJ, Bolam DN, Fontes CM J Biol Chem. 2006 Mar 31;281(13):8815-28. Epub 2005 Nov 28. PMID:16314409<ref>PMID:16314409</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2c4x" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_16314409}}, adds the Publication Abstract to the page
+*[[Glucanase 3D structures|Glucanase 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 16314409 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_16314409}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Acetivibrio thermocellus]]
-C4X is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_thermocellum Clostridium thermocellum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C4X OCA].
+[[Category: Large Structures]]
+[[Category: Alves VD]]
-==Reference==
+[[Category: Bolam DN]]
-Xyloglucan is recognized by carbohydrate-binding modules that interact with beta-glucan chains., Najmudin S, Guerreiro CI, Carvalho AL, Prates JA, Correia MA, Alves VD, Ferreira LM, Romao MJ, Gilbert HJ, Bolam DN, Fontes CM, J Biol Chem. 2006 Mar 31;281(13):8815-28. Epub 2005 Nov 28. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16314409 16314409]
+[[Category: Carvalho AL]]
-[[Category: Clostridium thermocellum]]
+[[Category: Correia MAS]]
-[[Category: Single protein]]
+[[Category: Ferreira LMA]]
-[[Category: Alves, V D.]]
+[[Category: Fontes CMGA]]
-[[Category: Bolam, D N.]]
+[[Category: Gilbert HJ]]
-[[Category: Carvalho, A L.]]
+[[Category: Guerreiro CIPD]]
-[[Category: Correia, M A.S.]]
+[[Category: Najmudin S]]
-[[Category: Ferreira, L M.A.]]
+[[Category: Prates JAM]]
-[[Category: Fontes, C M.G A.]]
+[[Category: Romao MJ]]
-[[Category: Gilbert, H J.]]
-[[Category: Guerreiro, C I.P D.]]
-[[Category: Najmudin, S.]]
-[[Category: Prates, J A.M.]]
-[[Category: Romao, M J.]]
-[[Category: Beta-sandwich protein]]
-[[Category: Carbohydrate binding module]]
-[[Category: Cbm44]]
-[[Category: Cellulase ctcel9d-cel44a]]
-[[Category: Cellulosome]]
-[[Category: Hydrolase]]
-[[Category: Pkd domain]]
-[[Category: Semet derivative]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:42:23 2008''