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<StructureSection load='1jg9' size='340' side='right'caption='[[1jg9]], [[Resolution|resolution]] 1.66&Aring;' scene=''>
<StructureSection load='1jg9' size='340' side='right'caption='[[1jg9]], [[Resolution|resolution]] 1.66&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1jg9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"neisseria_polysacchareae"_riou_et_al._1983 "neisseria polysacchareae" riou et al. 1983]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JG9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JG9 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1jg9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_polysaccharea Neisseria polysaccharea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JG9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JG9 FirstGlance]. <br>
</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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.66&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1jgi|1jgi]]</div></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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Amylosucrase Amylosucrase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.4 2.4.1.4] </span></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=1jg9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jg9 OCA], [https://pdbe.org/1jg9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jg9 RCSB], [https://www.ebi.ac.uk/pdbsum/1jg9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jg9 ProSAT]</span></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=1jg9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jg9 OCA], [https://pdbe.org/1jg9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jg9 RCSB], [https://www.ebi.ac.uk/pdbsum/1jg9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jg9 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/AMYS_NEIPO AMYS_NEIPO]] Catalyzes the synthesis of alpha-glucan from sucrose. Catalyzes, in addition, sucrose hydrolysis, maltose and maltotriose synthesis by successive transfers of the glucosyl moiety of sucrose onto the released glucose, and finally turanose and trehalulose synthesis, these two sucrose isomers being obtained by glucosyl transfer onto fructose.<ref>PMID:9882648</ref>
[https://www.uniprot.org/uniprot/AMYS_NEIPO AMYS_NEIPO] Catalyzes the synthesis of alpha-glucan from sucrose. Catalyzes, in addition, sucrose hydrolysis, maltose and maltotriose synthesis by successive transfers of the glucosyl moiety of sucrose onto the released glucose, and finally turanose and trehalulose synthesis, these two sucrose isomers being obtained by glucosyl transfer onto fructose.<ref>PMID:9882648</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1jg9 ConSurf].
</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=1jg9 ConSurf].
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<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The structure of amylosucrase from Neisseria polysaccharea in complex with beta-D-glucose has been determined by X-ray crystallography at a resolution of 1.66 A. Additionally, the structure of the inactive active site mutant Glu328Gln in complex with sucrose has been determined to a resolution of 2.0 A. The D-glucose complex shows two well-defined D-glucose molecules, one that binds very strongly in the bottom of a pocket that contains the proposed catalytic residues (at the subsite -1), in a nonstrained (4)C(1) conformation, and one that binds in the packing interface to a symmetry-related molecule. A third weaker D-glucose-binding site is located at the surface near the active site pocket entrance. The orientation of the D-glucose in the active site emphasizes the Glu328 role as the general acid/base. The binary sucrose complex shows one molecule bound in the active site, where the glucosyl moiety is located at the alpha-amylase -1 position and the fructosyl ring occupies subsite +1. Sucrose effectively blocks the only visible access channel to the active site. From analysis of the complex it appears that sucrose binding is primarily obtained through enzyme interactions with the glucosyl ring and that an important part of the enzyme function is a precise alignment of a lone pair of the linking O1 oxygen for hydrogen bond interaction with Glu328. The sucrose specificity appears to be determined primarily by residues Asp144, Asp394, Arg446, and Arg509. Both Asp394 and Arg446 are located in an insert connecting beta-strand 7 and alpha-helix 7 that is much longer in amylosucrase compared to other enzymes from the alpha-amylase family (family 13 of the glycoside hydrolases).
Crystal structures of amylosucrase from Neisseria polysaccharea in complex with D-glucose and the active site mutant Glu328Gln in complex with the natural substrate sucrose.,Mirza O, Skov LK, Remaud-Simeon M, Potocki de Montalk G, Albenne C, Monsan P, Gajhede M Biochemistry. 2001 Jul 31;40(30):9032-9. PMID:11467966<ref>PMID:11467966</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1jg9" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Neisseria polysacchareae riou et al. 1983]]
[[Category: Amylosucrase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Gajhede, M]]
[[Category: Neisseria polysaccharea]]
[[Category: Mirza, O]]
[[Category: Gajhede M]]
[[Category: Skov, L K]]
[[Category: Mirza O]]
[[Category: D-glucose complex]]
[[Category: Skov LK]]
[[Category: Transferase]]

Latest revision as of 07:39, 7 February 2024

Crystal Structure of Amylosucrase from Neisseria polysaccharea in Complex with D-glucose

1jg9, resolution 1.66Å

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