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==1.5 Angstrom Resolution Crystal Structure of K135M Mutant of Transaldolase B (TalA) from Francisella tularensis in Complex with Sedoheptulose 7-phosphate.== | ==1.5 Angstrom Resolution Crystal Structure of K135M Mutant of Transaldolase B (TalA) from Francisella tularensis in Complex with Sedoheptulose 7-phosphate.== | ||
<StructureSection load='3tkf' size='340' side='right' caption='[[3tkf]], [[Resolution|resolution]] 1.50Å' scene=''> | <StructureSection load='3tkf' size='340' side='right'caption='[[3tkf]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3tkf]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3tkf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"francisella_tularensis_subsp._nearctica"_olsufjev_1970 "francisella tularensis subsp. nearctica" olsufjev 1970]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TKF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TKF 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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=I22:D-ALTRO-HEPT-2-ULOSE+7-PHOSPHATE'>I22</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> | </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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=I22:D-ALTRO-HEPT-2-ULOSE+7-PHOSPHATE'>I22</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3igx|3igx]], [[3te9|3te9]], [[3tk7|3tk7]], [[4e0c|4e0c]], [[3tno|3tno]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3igx|3igx]], [[3te9|3te9]], [[3tk7|3tk7]], [[4e0c|4e0c]], [[3tno|3tno]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FTT_1093c, talA ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FTT_1093c, talA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=119856 "Francisella tularensis subsp. nearctica" Olsufjev 1970])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <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> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3tkf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tkf OCA], [https://pdbe.org/3tkf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tkf RCSB], [https://www.ebi.ac.uk/pdbsum/3tkf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tkf ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/Q5NFX0_FRATT Q5NFX0_FRATT]] Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway (By similarity).[RuleBase:RU004155][SAAS:SAAS004730_004_006516] | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 21: | Line 21: | ||
</div> | </div> | ||
<div class="pdbe-citations 3tkf" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3tkf" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Transaldolase 3D structures|Transaldolase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 26: | Line 29: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Francisella tularensis subsp. nearctica olsufjev 1970]] | [[Category: Francisella tularensis subsp. nearctica olsufjev 1970]] | ||
[[Category: Large Structures]] | |||
[[Category: Transaldolase]] | [[Category: Transaldolase]] | ||
[[Category: Anderson, W F]] | [[Category: Anderson, W F]] | ||
Revision as of 20:02, 6 July 2022
1.5 Angstrom Resolution Crystal Structure of K135M Mutant of Transaldolase B (TalA) from Francisella tularensis in Complex with Sedoheptulose 7-phosphate.1.5 Angstrom Resolution Crystal Structure of K135M Mutant of Transaldolase B (TalA) from Francisella tularensis in Complex with Sedoheptulose 7-phosphate.
Structural highlights
Function[Q5NFX0_FRATT] Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway (By similarity).[RuleBase:RU004155][SAAS:SAAS004730_004_006516] Publication Abstract from PubMedThe Burgi-Dunitz angle (alphaBD) describes the trajectory of approach of a nucleophile to an electrophile. The adoption of a stereoelectronically favorable alphaBD can necessitate significant reactive-group repositioning over the course of bond formation. In the context of enzyme catalysis, interactions with the protein constrain substrate rotation, which could necessitate structural transformations during bond formation. To probe this theoretical framework vis-a-vis biocatalysis, Schiff-base formation was analysed in Francisella tularensis transaldolase (TAL). Crystal structures of wild-type and Lys-->Met mutant TAL in covalent and noncovalent complexes with fructose 6-phosphate and sedoheptulose 7-phosphate clarify the mechanism of catalysis and reveal that substrate keto moieties undergo significant conformational changes during Schiff-base formation. Structural changes compelled by the trajectory considerations discussed here bear relevance to bond formation in a variety of constrained enzymic/engineered systems and can inform the design of covalent therapeutics. Adherence to Burgi-Dunitz stereochemical principles requires significant structural rearrangements in Schiff-base formation: insights from transaldolase complexes.,Light SH, Minasov G, Duban ME, Anderson WF Acta Crystallogr D Biol Crystallogr. 2014 Feb;70(Pt 2):544-52. doi:, 10.1107/S1399004713030666. Epub 2014 Jan 31. PMID:24531488[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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