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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]] 1.80&Aring;' scene=''>
<StructureSection load='4e0c' size='340' side='right'caption='[[4e0c]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4e0c]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Fratt Fratt]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E0C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E0C FirstGlance]. <br>
<table><tr><td colspan='2'>[[4e0c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Francisella_tularensis_subsp._tularensis_SCHU_S4 Francisella tularensis subsp. tularensis SCHU S4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E0C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E0C FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br>
</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>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3igx|3igx]], [[3tk7|3tk7]], [[3tno|3tno]], [[3upb|3upb]], [[3te9|3te9]], [[3tkf|3tkf]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
<tr><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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4e0c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e0c OCA], [https://pdbe.org/4e0c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e0c RCSB], [https://www.ebi.ac.uk/pdbsum/4e0c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e0c ProSAT]</span></td></tr>
<tr><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>
</table>
<tr><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>
== Function ==
<table>
[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;">
== Publication Abstract from PubMed ==
The 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--&gt;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<ref>PMID:24531488</ref>


From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
==See Also==
</div>
*[[Transaldolase 3D structures|Transaldolase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Fratt]]
[[Category: Francisella tularensis subsp. tularensis SCHU S4]]
[[Category: Transaldolase]]
[[Category: Large Structures]]
[[Category: Anderson, W F.]]
[[Category: Anderson WF]]
[[Category: CSGID, Center for Structural Genomics of Infectious Diseases.]]
[[Category: Halavaty AS]]
[[Category: Halavaty, A S.]]
[[Category: Light SH]]
[[Category: Light, S H.]]
[[Category: Minasov G]]
[[Category: Minasov, G.]]
[[Category: Papazisi L]]
[[Category: Papazisi, L.]]
[[Category: Shuvalova L]]
[[Category: Shuvalova, L.]]
[[Category: Alpha-beta barrel/tim barrel]]
[[Category: Center for structural genomics of infectious disease]]
[[Category: Csgid]]
[[Category: National institute of allergy and infectious disease]]
[[Category: Niaid]]
[[Category: Structural genomic]]
[[Category: Transferase]]

Latest revision as of 17:49, 14 March 2024

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

4e0c is a 2 chain structure with sequence from Francisella tularensis subsp. tularensis SCHU S4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q5NFX0_FRATT Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway (By similarity).[RuleBase:RU004155][SAAS:SAAS004730_004_006516]

See Also

4e0c, resolution 1.80Å

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