3s1w

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Current revision (12:43, 14 March 2024) (edit) (undo)
 
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<StructureSection load='3s1w' size='340' side='right'caption='[[3s1w]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='3s1w' size='340' side='right'caption='[[3s1w]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3s1w]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Theac Theac]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S1W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3S1W FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3s1w]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermoplasma_acidophilum_DSM_1728 Thermoplasma acidophilum DSM 1728]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S1W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3S1W FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3s0c|3s0c]], [[3s1u|3s1u]], [[3s1v|3s1v]], [[3s1x|3s1x]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Ta0616, tal ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273075 THEAC])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Transaldolase Transaldolase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.2.1.2 2.2.1.2] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3s1w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s1w OCA], [https://pdbe.org/3s1w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3s1w RCSB], [https://www.ebi.ac.uk/pdbsum/3s1w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3s1w 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=3s1w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s1w OCA], [https://pdbe.org/3s1w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3s1w RCSB], [https://www.ebi.ac.uk/pdbsum/3s1w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3s1w ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/TAL_THEAC TAL_THEAC]] Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
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[https://www.uniprot.org/uniprot/TAL_THEAC TAL_THEAC] Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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We examined the catalytic cycle of transaldolase (TAL) from Thermoplasma acidophilum by cryocrystallography and were able to structurally characterize-for the first time, to our knowledge-different genuine TAL reaction intermediates. These include the Schiff base adducts formed between the catalytic lysine and the donor ketose substrates fructose-6-phosphate and sedoheptulose-7-phosphate as well as the Michaelis complex with acceptor aldose erythrose-4-phosphate. These structural snapshots necessitate a revision of the accepted reaction mechanism with respect to functional roles of active site residues, and they further reveal fundamental insights into the general structural features of enzymatic Schiff base intermediates and the role of conformational dynamics in enzyme catalysis, substrate binding and discrimination. A nonplanar arrangement of the substituents around the Schiff base double bond was observed, suggesting that a structurally encoded reactant-state destabilization is a driving force of catalysis. Protein dynamics and the intrinsic hydrogen-bonding pattern appear to be crucial for selective recognition and binding of ketose as first substrate.
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Twisted Schiff base intermediates and substrate locale revise transaldolase mechanism.,Lehwess-Litzmann A, Neumann P, Parthier C, Ludtke S, Golbik R, Ficner R, Tittmann K Nat Chem Biol. 2011 Aug 21. doi: 10.1038/nchembio.633. PMID:21857661<ref>PMID:21857661</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3s1w" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Theac]]
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[[Category: Thermoplasma acidophilum DSM 1728]]
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[[Category: Transaldolase]]
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[[Category: Lehwess-Litzmann A]]
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[[Category: Lehwess-Litzmann, A]]
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[[Category: Neumann P]]
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[[Category: Neumann, P]]
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[[Category: Parthier C]]
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[[Category: Parthier, C]]
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[[Category: Tittmann K]]
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[[Category: Tittmann, K]]
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[[Category: Alpha-beta barrel]]
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[[Category: Conformational selection]]
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[[Category: Domain swapping]]
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[[Category: Protein dynamic]]
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[[Category: Transferase]]
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Current revision

Transaldolase variant Lys86Ala from Thermoplasma acidophilum in complex with glycerol and citrate

PDB ID 3s1w

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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