2j72

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[[Image:2j72.jpg|left|200px]]<br /><applet load="2j72" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2j72, resolution 1.49&Aring;" />
 
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'''ALPHA-GLUCAN RECOGNITION BY A FAMILY 41 CARBOHYDRATE-BINDING MODULE FROM THERMOTOGA MARITIMA PULLULANASE PULA'''<br />
 
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==About this Structure==
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==alpha-glucan recognition by a family 41 carbohydrate-binding module from Thermotoga maritima pullulanase PulA==
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2J72 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Active as [http://en.wikipedia.org/wiki/Pullulanase Pullulanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.41 3.2.1.41] Known structural/functional Site: <scene name='pdbsite=AC1:Glc+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J72 OCA].
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<StructureSection load='2j72' size='340' side='right'caption='[[2j72]], [[Resolution|resolution]] 1.49&Aring;' scene=''>
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[[Category: Pullulanase]]
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== Structural highlights ==
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[[Category: Single protein]]
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<table><tr><td colspan='2'>[[2j72]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J72 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J72 FirstGlance]. <br>
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[[Category: Thermotoga maritima]]
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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]] 1.49&#8491;</td></tr>
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[[Category: Boraston, A B.]]
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900010:alpha-maltotetraose'>PRD_900010</scene></td></tr>
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[[Category: Bueren, A Lammerts Van.]]
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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=2j72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j72 OCA], [https://pdbe.org/2j72 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j72 RCSB], [https://www.ebi.ac.uk/pdbsum/2j72 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j72 ProSAT]</span></td></tr>
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[[Category: alpha-glucan binding]]
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</table>
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[[Category: beta- sandwich fold]]
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== Function ==
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[[Category: carbohydrate-binding module]]
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[https://www.uniprot.org/uniprot/PULA_THEMA PULA_THEMA]
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[[Category: glycosidase]]
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== Evolutionary Conservation ==
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[[Category: hydrolase]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: maltotetraose]]
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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/j7/2j72_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=2j72 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Starch recognition by carbohydrate-binding modules (CBMs) is important for the activity of starch-degrading enzymes. The N-terminal family 41 CBM, TmCBM41 (from pullulanase PulA secreted by Thermotoga maritima) was shown to have alpha-glucan binding activity with specificity for alpha-1,4-glucans but was able to tolerate the alpha-1,6-linkages found roughly every three or four glucose units in pullulan. Using X-ray crystallography, the structures were solved for TmCBM41 in an uncomplexed form and in complex with maltotetraose and 6(3)-alpha-D-glucosyl-maltotriose (GM3). Ligand binding was facilitated by stacking interactions between the alpha-faces of the glucose residues and two tryptophan side-chains in the two main subsites of the carbohydrate-binding site. Overall, this mode of starch binding is quite well conserved by other starch-binding modules. The structure in complex with GM3 revealed a third binding subsite with the flexibility to accommodate an alpha-1,4- or an alpha-1,6-linked glucose.
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:59:58 2008''
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The structural basis of alpha-glucan recognition by a family 41 carbohydrate-binding module from Thermotoga maritima.,van Bueren AL, Boraston AB J Mol Biol. 2007 Jan 19;365(3):555-60. Epub 2006 Oct 11. PMID:17095014<ref>PMID:17095014</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2j72" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Thermotoga maritima]]
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[[Category: Boraston AB]]
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[[Category: Lammerts van Bueren A]]

Current revision

alpha-glucan recognition by a family 41 carbohydrate-binding module from Thermotoga maritima pullulanase PulA

PDB ID 2j72

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