1g5a: Difference between revisions

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<StructureSection load='1g5a' size='340' side='right'caption='[[1g5a]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
<StructureSection load='1g5a' size='340' side='right'caption='[[1g5a]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1g5a]] is a 1 chain structure with sequence from [http://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=1G5A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G5A FirstGlance]. <br>
<table><tr><td colspan='2'>[[1g5a]] 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=1G5A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G5A FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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]] 1.4&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Amylosucrase Amylosucrase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.4 2.4.1.4] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></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=1g5a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g5a OCA], [http://pdbe.org/1g5a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1g5a RCSB], [http://www.ebi.ac.uk/pdbsum/1g5a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1g5a 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=1g5a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g5a OCA], [https://pdbe.org/1g5a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g5a RCSB], [https://www.ebi.ac.uk/pdbsum/1g5a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g5a ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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=1g5a 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=1g5a ConSurf].
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== Publication Abstract from PubMed ==
Amylosucrase (E.C. 2.4.1.4) is a member of Family 13 of the glycoside hydrolases (the alpha-amylases), although its biological function is the synthesis of amylose-like polymers from sucrose. The structure of amylosucrase from Neisseria polysaccharea is divided into five domains: an all helical N-terminal domain that is not similar to any known fold, a (beta/alpha)(8)-barrel A-domain, B- and B'-domains displaying alpha/beta-structure, and a C-terminal eight-stranded beta-sheet domain. In contrast to other Family 13 hydrolases that have the active site in the bottom of a large cleft, the active site of amylosucrase is at the bottom of a pocket at the molecular surface. A substrate binding site resembling the amylase 2 subsite is not found in amylosucrase. The site is blocked by a salt bridge between residues in the second and eight loops of the (beta/alpha)(8)-barrel. The result is an exo-acting enzyme. Loop 7 in the amylosucrase barrel is prolonged compared with the loop structure found in other hydrolases, and this insertion (forming domain B') is suggested to be important for the polymer synthase activity of the enzyme. The topology of the B'-domain creates an active site entrance with several ravines in the molecular surface that could be used specifically by the substrates/products (sucrose, glucan polymer, and fructose) that have to get in and out of the active site pocket.
Amylosucrase, a glucan-synthesizing enzyme from the alpha-amylase family.,Skov LK, Mirza O, Henriksen A, De Montalk GP, Remaud-Simeon M, Sarcabal P, Willemot RM, Monsan P, Gajhede M J Biol Chem. 2001 Jul 6;276(27):25273-8. Epub 2001 Apr 16. PMID:11306569<ref>PMID:11306569</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1g5a" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__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: Henriksen, A]]
[[Category: De Montalk GP]]
[[Category: Mirza, O]]
[[Category: Gajhede M]]
[[Category: Monsan, P]]
[[Category: Henriksen A]]
[[Category: Montalk, G P.De]]
[[Category: Mirza O]]
[[Category: Remaud-Simeon, M]]
[[Category: Monsan P]]
[[Category: Sarcabal, P]]
[[Category: Remaud-Simeon M]]
[[Category: Skov, L K]]
[[Category: Sarcabal P]]
[[Category: Willemot, R M]]
[[Category: Skov LK]]
[[Category: Glycoside hydrolase]]
[[Category: Willemot R-M]]
[[Category: Glycosyltransferase]]
[[Category: Transferase]]

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