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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=''> | ||
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FTT_1093c, talA ([http://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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FTT_1093c, talA ([http://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'>[http://en.wikipedia.org/wiki/Transaldolase Transaldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.2.1.2 2.2.1.2] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transaldolase Transaldolase], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3tkf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tkf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tkf RCSB], [http://www.ebi.ac.uk/pdbsum/3tkf PDBsum]</span></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=3tkf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tkf OCA], [http://pdbe.org/3tkf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3tkf RCSB], [http://www.ebi.ac.uk/pdbsum/3tkf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3tkf ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3tkf" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
Revision as of 03:07, 5 August 2016
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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