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[[Image:2d3n.gif|left|200px]]
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{{STRUCTURE_2d3n|  PDB=2d3n  |  SCENE=  }}
'''Crystal structure of maltohexaose-producing amylase from Bacillus sp.707 complexed with maltohexaose'''


==Crystal structure of maltohexaose-producing amylase from Bacillus sp.707 complexed with maltohexaose==
<StructureSection load='2d3n' size='340' side='right'caption='[[2d3n]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2d3n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_sp._707 Bacillus sp. 707]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D3N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2D3N FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</scene>, <scene name='pdbligand=PRD_900009:alpha-maltotriose'>PRD_900009</scene>, <scene name='pdbligand=PRD_900010:alpha-maltotetraose'>PRD_900010</scene>, <scene name='pdbligand=PRD_900035:alpha-maltohexaose'>PRD_900035</scene></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=2d3n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d3n OCA], [https://pdbe.org/2d3n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2d3n RCSB], [https://www.ebi.ac.uk/pdbsum/2d3n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2d3n ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AMT6_BACS7 AMT6_BACS7]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d3/2d3n_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </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/main_output.php?pdb_ID=2d3n ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Maltohexaose-producing amylase (G6-amylase) from alkalophilic Bacillus sp.707 predominantly produces maltohexaose (G6) in the yield of &gt;30% of the total products from short-chain amylose (DP=17). Our previous crystallographic study showed that G6-amylase has nine subsites, from -6 to +3, and pointed out the importance of the indole moiety of Trp140 in G6 production. G6-amylase has very low levels of hydrolytic activities for oligosaccharides shorter than maltoheptaose. To elucidate the mechanism underlying G6 production, we determined the crystal structures of the G6-amylase complexes with G6 and maltopentaose (G5). In the active site of the G6-amylase/G5 complex, G5 is bound to subsites -6 to -2, while G1 and G6 are found at subsites +2 and -7 to -2, respectively, in the G6-amylase/G6 complex. In both structures, the glucosyl residue located at subsite -6 is stacked to the indole moiety of Trp140 within a distance of 4A. The measurement of the activities of the mutant enzymes when Trp140 was replaced by leucine (W140L) or by tyrosine (W140Y) showed that the G6 production from short-chain amylose by W140L is lower than that by W140Y or wild-type enzyme. The face-to-face short contact between Trp140 and substrate sugars is suggested to regulate the disposition of the glucosyl residue at subsite -6 and to govern product specificity for G6 production.


==Overview==
Role of Trp140 at subsite -6 on the maltohexaose production of maltohexaose-producing amylase from alkalophilic Bacillus sp.707.,Kanai R, Haga K, Akiba T, Yamane K, Harata K Protein Sci. 2006 Mar;15(3):468-77. Epub 2006 Feb 1. PMID:16452622<ref>PMID:16452622</ref>
Maltohexaose-producing amylase (G6-amylase) from alkalophilic Bacillus sp.707 predominantly produces maltohexaose (G6) in the yield of &gt;30% of the total products from short-chain amylose (DP=17). Our previous crystallographic study showed that G6-amylase has nine subsites, from -6 to +3, and pointed out the importance of the indole moiety of Trp140 in G6 production. G6-amylase has very low levels of hydrolytic activities for oligosaccharides shorter than maltoheptaose. To elucidate the mechanism underlying G6 production, we determined the crystal structures of the G6-amylase complexes with G6 and maltopentaose (G5). In the active site of the G6-amylase/G5 complex, G5 is bound to subsites -6 to -2, while G1 and G6 are found at subsites +2 and -7 to -2, respectively, in the G6-amylase/G6 complex. In both structures, the glucosyl residue located at subsite -6 is stacked to the indole moiety of Trp140 within a distance of 4A. The measurement of the activities of the mutant enzymes when Trp140 was replaced by leucine (W140L) or by tyrosine (W140Y) showed that the G6 production from short-chain amylose by W140L is lower than that by W140Y or wild-type enzyme. The face-to-face short contact between Trp140 and substrate sugars is suggested to regulate the disposition of the glucosyl residue at subsite -6 and to govern product specificity for G6 production.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2D3N is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_sp. Bacillus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D3N OCA].
</div>
<div class="pdbe-citations 2d3n" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Role of Trp140 at subsite -6 on the maltohexaose production of maltohexaose-producing amylase from alkalophilic Bacillus sp.707., Kanai R, Haga K, Akiba T, Yamane K, Harata K, Protein Sci. 2006 Mar;15(3):468-77. Epub 2006 Feb 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16452622 16452622]
*[[Amylase 3D structures|Amylase 3D structures]]
[[Category: Bacillus sp.]]
== References ==
[[Category: Glucan 1,4-alpha-maltohexaosidase]]
<references/>
[[Category: Single protein]]
__TOC__
[[Category: Akiba, T.]]
</StructureSection>
[[Category: Haga, K.]]
[[Category: Bacillus sp. 707]]
[[Category: Harata, K.]]
[[Category: Large Structures]]
[[Category: Kanai, R.]]
[[Category: Akiba T]]
[[Category: Yamane, K.]]
[[Category: Haga K]]
[[Category: Ligand binding]]
[[Category: Harata K]]
[[Category: Maltohexaose]]
[[Category: Kanai R]]
[[Category: Protein-carbohydrate complex]]
[[Category: Yamane K]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 23:38:33 2008''

Latest revision as of 11:23, 25 October 2023

Crystal structure of maltohexaose-producing amylase from Bacillus sp.707 complexed with maltohexaoseCrystal structure of maltohexaose-producing amylase from Bacillus sp.707 complexed with maltohexaose

Structural highlights

2d3n is a 1 chain structure with sequence from Bacillus sp. 707. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:, , , , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AMT6_BACS7

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

Maltohexaose-producing amylase (G6-amylase) from alkalophilic Bacillus sp.707 predominantly produces maltohexaose (G6) in the yield of >30% of the total products from short-chain amylose (DP=17). Our previous crystallographic study showed that G6-amylase has nine subsites, from -6 to +3, and pointed out the importance of the indole moiety of Trp140 in G6 production. G6-amylase has very low levels of hydrolytic activities for oligosaccharides shorter than maltoheptaose. To elucidate the mechanism underlying G6 production, we determined the crystal structures of the G6-amylase complexes with G6 and maltopentaose (G5). In the active site of the G6-amylase/G5 complex, G5 is bound to subsites -6 to -2, while G1 and G6 are found at subsites +2 and -7 to -2, respectively, in the G6-amylase/G6 complex. In both structures, the glucosyl residue located at subsite -6 is stacked to the indole moiety of Trp140 within a distance of 4A. The measurement of the activities of the mutant enzymes when Trp140 was replaced by leucine (W140L) or by tyrosine (W140Y) showed that the G6 production from short-chain amylose by W140L is lower than that by W140Y or wild-type enzyme. The face-to-face short contact between Trp140 and substrate sugars is suggested to regulate the disposition of the glucosyl residue at subsite -6 and to govern product specificity for G6 production.

Role of Trp140 at subsite -6 on the maltohexaose production of maltohexaose-producing amylase from alkalophilic Bacillus sp.707.,Kanai R, Haga K, Akiba T, Yamane K, Harata K Protein Sci. 2006 Mar;15(3):468-77. Epub 2006 Feb 1. PMID:16452622[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Kanai R, Haga K, Akiba T, Yamane K, Harata K. Role of Trp140 at subsite -6 on the maltohexaose production of maltohexaose-producing amylase from alkalophilic Bacillus sp.707. Protein Sci. 2006 Mar;15(3):468-77. Epub 2006 Feb 1. PMID:16452622 doi:http://dx.doi.org/10.1110/ps.051877006

2d3n, resolution 1.90Å

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