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1nbc

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[[Image:1nbc.gif|left|200px]]
 
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{{Structure
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==BACTERIAL TYPE 3A CELLULOSE-BINDING DOMAIN==
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|PDB= 1nbc |SIZE=350|CAPTION= <scene name='initialview01'>1nbc</scene>, resolution 1.75&Aring;
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<StructureSection load='1nbc' size='340' side='right'caption='[[1nbc]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>
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<table><tr><td colspan='2'>[[1nbc]] is a 2 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=1NBC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NBC FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
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|GENE= CIPB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1515 Clostridium thermocellum])
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<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>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1nbc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nbc OCA], [https://pdbe.org/1nbc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nbc RCSB], [https://www.ebi.ac.uk/pdbsum/1nbc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nbc ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nbc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nbc OCA], [http://www.ebi.ac.uk/pdbsum/1nbc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nbc RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/CIPA_ACET2 CIPA_ACET2] Acts as a scaffolding protein in the cellulosome. It promotes binding of cellulose to the catalytic domains of the cellulolytic enzymes.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nb/1nbc_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1nbc ConSurf].
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<div style="clear:both"></div>
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'''BACTERIAL TYPE 3A CELLULOSE-BINDING DOMAIN'''
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==See Also==
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*[[Cellulosomal scaffolding protein|Cellulosomal scaffolding protein]]
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*[[Cellulosome scaffolding protein 3D structures|Cellulosome scaffolding protein 3D structures]]
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==Overview==
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__TOC__
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The crystal structure of a family-III cellulose-binding domain (CBD) from the cellulosomal scaffoldin subunit of Clostridium thermocellum has been determined at 1.75 A resolution. The protein forms a nine-stranded beta sandwich with a jelly roll topology and binds a calcium ion. conserved, surface-exposed residues map into two defined surfaces located on opposite sides of the molecule. One of these faces is dominated by a planar linear strip of aromatic and polar residues which are proposed to interact with crystalline cellulose. The other conserved residues are contained in a shallow groove, the function of which is currently unknown, and which has not been observed previously in other families of CBDs. On the basis of modeling studies combined with comparisons of recently determined NMR structures for other CBDs, a general model for the binding of CBDs to cellulose is presented. Although the proposed binding of the CBD to cellulose is essentially a surface interaction, specific types and combinations of amino acids appear to interact selectively with glucose moieties positioned on three adjacent chains of the cellulose surface. The major interaction is characterized by the planar strip of aromatic residues, which align along one of the chains. In addition, polar amino acid residues are proposed to anchor the CBD molecule to two other adjacent chains of crystalline cellulose.
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</StructureSection>
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[[Category: Acetivibrio thermocellus]]
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==About this Structure==
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[[Category: Large Structures]]
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1NBC 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=1NBC OCA].
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[[Category: Lamed R]]
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[[Category: Steitz TA]]
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==Reference==
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[[Category: Tormo J]]
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Crystal structure of a bacterial family-III cellulose-binding domain: a general mechanism for attachment to cellulose., Tormo J, Lamed R, Chirino AJ, Morag E, Bayer EA, Shoham Y, Steitz TA, EMBO J. 1996 Nov 1;15(21):5739-51. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8918451 8918451]
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[[Category: Clostridium thermocellum]]
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[[Category: Single protein]]
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[[Category: Lamed, R.]]
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[[Category: Steitz, T A.]]
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[[Category: Tormo, J.]]
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[[Category: cellulose degradation]]
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[[Category: cellulose-binding domain]]
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[[Category: cellulosome]]
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[[Category: scafoldin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:28:02 2008''
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Current revision

BACTERIAL TYPE 3A CELLULOSE-BINDING DOMAIN

PDB ID 1nbc

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