4e0c: Difference between revisions
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==1.8 Angstrom Resolution Crystal Structure of Transaldolase from Francisella tularensis (phosphate-free)== | ==1.8 Angstrom Resolution Crystal Structure of Transaldolase from Francisella tularensis (phosphate-free)== | ||
<StructureSection load='4e0c' size='340' side='right' caption='[[4e0c]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='4e0c' size='340' side='right' caption='[[4e0c]], [[Resolution|resolution]] 1.80Å' 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=177416 FRATT])</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=177416 FRATT])</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=4e0c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e0c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4e0c RCSB], [http://www.ebi.ac.uk/pdbsum/4e0c 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=4e0c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e0c OCA], [http://pdbe.org/4e0c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4e0c RCSB], [http://www.ebi.ac.uk/pdbsum/4e0c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4e0c 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 4e0c" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
Revision as of 15:43, 5 August 2016
1.8 Angstrom Resolution Crystal Structure of Transaldolase from Francisella tularensis (phosphate-free)1.8 Angstrom Resolution Crystal Structure of Transaldolase from Francisella tularensis (phosphate-free)
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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