2j72: Difference between revisions
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==alpha-glucan recognition by a family 41 carbohydrate-binding module from Thermotoga maritima pullulanase PulA== | |||
<StructureSection load='2j72' size='340' side='right' caption='[[2j72]], [[Resolution|resolution]] 1.49Å' scene=''> | <StructureSection load='2j72' size='340' side='right' caption='[[2j72]], [[Resolution|resolution]] 1.49Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2j71|2j71]], [[2j73|2j73]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2j71|2j71]], [[2j73|2j73]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </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=2j72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j72 OCA], [http://pdbe.org/2j72 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2j72 RCSB], [http://www.ebi.ac.uk/pdbsum/2j72 PDBsum]</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=2j72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j72 OCA], [http://pdbe.org/2j72 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2j72 RCSB], [http://www.ebi.ac.uk/pdbsum/2j72 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2j72 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j7/2j72_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j7/2j72_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | </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]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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[[Category: Pullulanase]] | [[Category: Pullulanase]] | ||
[[Category: Boraston, A B]] | [[Category: Boraston, A B]] | ||
[[Category: Bueren, A Lammerts | [[Category: Bueren, A Lammerts van]] | ||
[[Category: Alpha-glucan binding]] | [[Category: Alpha-glucan binding]] | ||
[[Category: Beta- sandwich fold]] | [[Category: Beta- sandwich fold]] |
Revision as of 09:29, 11 July 2018
alpha-glucan recognition by a family 41 carbohydrate-binding module from Thermotoga maritima pullulanase PulAalpha-glucan recognition by a family 41 carbohydrate-binding module from Thermotoga maritima pullulanase PulA
Structural highlights
Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedStarch 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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