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| | <StructureSection load='2c3v' size='340' side='right'caption='[[2c3v]], [[Resolution|resolution]] 1.39Å' scene=''> | | <StructureSection load='2c3v' size='340' side='right'caption='[[2c3v]], [[Resolution|resolution]] 1.39Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2c3v]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bachd Bachd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C3V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C3V FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2c3v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Alkalihalobacillus_halodurans_C-125 Alkalihalobacillus halodurans C-125]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C3V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C3V FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.39Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TYI:3,5-DIIODOTYROSINE'>TYI</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=TYI:3,5-DIIODOTYROSINE'>TYI</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2c3g|2c3g]], [[2c3h|2c3h]], [[2c3w|2c3w]], [[2c3x|2c3x]]</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2c3v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c3v OCA], [https://pdbe.org/2c3v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c3v RCSB], [https://www.ebi.ac.uk/pdbsum/2c3v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c3v ProSAT]</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=2c3v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c3v OCA], [http://pdbe.org/2c3v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2c3v RCSB], [http://www.ebi.ac.uk/pdbsum/2c3v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2c3v ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9KFR4_HALH5 Q9KFR4_HALH5] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c3/2c3v_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c3/2c3v_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bachd]] | + | [[Category: Alkalihalobacillus halodurans C-125]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Boraston, A B]] | + | [[Category: Boraston AB]] |
| - | [[Category: Bueren, A Lammerts van]]
| + | [[Category: Ficko-Blean E]] |
| - | [[Category: Ficko-Blean, E]] | + | [[Category: Healey M]] |
| - | [[Category: Healey, M]] | + | [[Category: Klassen J]] |
| - | [[Category: Klassen, J]] | + | [[Category: Lammerts van Bueren A]] |
| - | [[Category: Law, V]] | + | [[Category: Law V]] |
| - | [[Category: Amylopectin]] | + | |
| - | [[Category: Amylose]]
| + | |
| - | [[Category: Carbohydrate binding]]
| + | |
| - | [[Category: Carbohydrate- binding module]]
| + | |
| - | [[Category: Carbohydrate-binding module]]
| + | |
| - | [[Category: Glycoside hydrolase]]
| + | |
| - | [[Category: Malto-oligosaccharide]]
| + | |
| - | [[Category: Starch binding]]
| + | |
| Structural highlights
Function
Q9KFR4_HALH5
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-hydrolyzing enzymes lacking alpha-glucan-specific carbohydrate-binding modules (CBMs) typically have lowered activity on granular starch relative to their counterparts with CBMs. Thus, consideration of starch recognition by CBMs is a key factor in understanding granular starch hydrolysis. To this end, we have dissected the modular structure of the maltohexaose-forming amylase from Bacillus halodurans (C-125). This five-module protein comprises an N-terminal family 13 catalytic module followed in order by two modules of unknown function, a family 26 CBM (BhCBM26), and a family 25 CBM (BhCBM25). Here we present a comprehensive structure-function analysis of starch and alpha-glucooligosaccharide recognition by BhCBM25 and BhCBM26 using UV methods, isothermal titration calorimetry, and x-ray crystallography. The results reveal that the two CBMs bind alpha-glucooligosaccharides, particularly those containing alpha-1,6 linkages, with different affinities but have similar abilities to bind granular starch. Notably, these CBMs appear to recognize the same binding sites in granular starch. The enhanced affinity of the tandem CBMs for granular starch is suggested to be the main biological advantage for this enzyme to contain two CBMs. Structural studies of the native and ligand-bound forms of BhCBM25 and BhCBM26 show a structurally conserved mode of ligand recognition but through non-sequence-conserved residues. Comparison of these CBM structures with other starch-specific CBM structures reveals a generally conserved mode of starch recognition.
A structural and functional analysis of alpha-glucan recognition by family 25 and 26 carbohydrate-binding modules reveals a conserved mode of starch recognition.,Boraston AB, Healey M, Klassen J, Ficko-Blean E, Lammerts van Bueren A, Law V J Biol Chem. 2006 Jan 6;281(1):587-98. Epub 2005 Oct 17. PMID:16230347[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Boraston AB, Healey M, Klassen J, Ficko-Blean E, Lammerts van Bueren A, Law V. A structural and functional analysis of alpha-glucan recognition by family 25 and 26 carbohydrate-binding modules reveals a conserved mode of starch recognition. J Biol Chem. 2006 Jan 6;281(1):587-98. Epub 2005 Oct 17. PMID:16230347 doi:10.1074/jbc.M509958200
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