5zol
From Proteopedia
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<StructureSection load='5zol' size='340' side='right'caption='[[5zol]], [[Resolution|resolution]] 2.17Å' scene=''> | <StructureSection load='5zol' size='340' side='right'caption='[[5zol]], [[Resolution|resolution]] 2.17Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5zol]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZOL OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[5zol]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZOL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZOL FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4Y8:1-HYDROXYPROPAN-2-ONE'>4Y8</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=LW1:thiophene-2-carbaldehyde'>LW1</scene>, <scene name='pdbligand=LW2:( | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.172Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4Y8:1-HYDROXYPROPAN-2-ONE'>4Y8</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=LW1:thiophene-2-carbaldehyde'>LW1</scene>, <scene name='pdbligand=LW2:(3~{S},4~{S})-3,4-bis(oxidanyl)-4-thiophen-2-yl-butan-2-one'>LW2</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5zol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zol OCA], [https://pdbe.org/5zol PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zol RCSB], [https://www.ebi.ac.uk/pdbsum/5zol PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zol ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/FSAA_ECOLI FSAA_ECOLI] Catalyzes the reversible formation of fructose 6-phosphate from dihydroxyacetone (DHA) and D-glyceraldehyde 3-phosphate via an aldolization reaction. Can utilize several aldehydes as acceptor compounds in vitro, and hydroxyacetone (HA) or 1-hydroxy-butan-2-one as alternative donor substrate. Is also able to catalyze the direct stereoselective self-aldol addition of glycolaldehyde to furnish D-(-)-threose, and cross-aldol reactions of glycolaldehyde to other aldehyde acceptors. Is not able to cleave fructose, fructose 1-phosphate, glucose 6-phosphate, sedoheptulose 1,7-bisphosphate, xylulose 5-phosphate, ribulose 5-phosphate, and fructose 1,6-bisphosphate; cannot use dihydroxyacetone phosphate as donor compound nor D-glyceraldehyde as acceptor. Does not display transaldolase activity.<ref>PMID:11120740</ref> [HAMAP-Rule:MF_00496]<ref>PMID:17985886</ref> <ref>PMID:19554584</ref> |
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The combinatorial modulation of inter- and intra-subunit interactions of decameric d-fructose-6-phosphate aldolase A (FSAA) generated a triple-site variant I31T/Q59T/I195Q FSAA with 27- to 278-fold improvement in activity towards target heteroaromatic aldehydes. X-ray crystallographic data and molecular dynamics simulations ascribed the enhanced activity to the pronounced flexibility of the interface region between subunits, the expanded substrate entrance and binding pocket, and enhanced proton transfer, unambiguously demonstrating the efficiency of this strategy for engineering multimeric enzymes. | ||
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| + | The engineering of decameric d-fructose-6-phosphate aldolase A by combinatorial modulation of inter- and intra-subunit interactions.,Yang X, Wu L, Li A, Ye L, Zhou J, Yu H Chem Commun (Camb). 2020 Jul 14;56(55):7561-7564. doi: 10.1039/d0cc02437f. Epub, 2020 Jun 10. PMID:32519699<ref>PMID:32519699</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5zol" style="background-color:#fffaf0;"></div> | ||
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| + | ==See Also== | ||
| + | *[[Aldolase 3D structures|Aldolase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Escherichia coli K-12]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Wu | + | [[Category: Wu L]] |
| - | [[Category: Yang | + | [[Category: Yang XH]] |
| - | [[Category: Yu | + | [[Category: Yu HW]] |
| - | [[Category: Zhou | + | [[Category: Zhou JH]] |
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Current revision
Crystal structure of a three sites mutantion of FSAA complexed with HA and product
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