2j72: Difference between revisions

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==alpha-glucan recognition by a family 41 carbohydrate-binding module from Thermotoga maritima pullulanase PulA==
==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]] 1.49&Aring;' scene=''>
<StructureSection load='2j72' size='340' side='right'caption='[[2j72]], [[Resolution|resolution]] 1.49&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2j72]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2J72 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2j72]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. 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 [http://proteopedia.org/fgij/fg.htm?mol=2J72 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene></td></tr>
</td></tr><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></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='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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2j72 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/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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</StructureSection>
</StructureSection>
[[Category: Atcc 43589]]
[[Category: Atcc 43589]]
[[Category: Large Structures]]
[[Category: Pullulanase]]
[[Category: Pullulanase]]
[[Category: Boraston, A B]]
[[Category: Boraston, A B]]

Revision as of 10:42, 15 April 2020

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

2j72 is a 2 chain structure with sequence from Atcc 43589. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Activity:Pullulanase, with EC number 3.2.1.41
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 PubMed

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.

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

  1. van Bueren AL, Boraston AB. The structural basis of alpha-glucan recognition by a family 41 carbohydrate-binding module from Thermotoga maritima. J Mol Biol. 2007 Jan 19;365(3):555-60. Epub 2006 Oct 11. PMID:17095014 doi:10.1016/j.jmb.2006.10.018

2j72, resolution 1.49Å

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