3te9: Difference between revisions

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<StructureSection load='3te9' size='340' side='right'caption='[[3te9]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='3te9' size='340' side='right'caption='[[3te9]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3te9]] 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=3TE9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TE9 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3te9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Francisella_tularensis_subsp._tularensis Francisella tularensis subsp. tularensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TE9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TE9 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=F6R:FRUCTOSE+-6-PHOSPHATE'>F6R</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
</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 id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3igx|3igx]], [[4e0c|4e0c]], [[3tk7|3tk7]], [[3tno|3tno]], [[3tkf|3tkf]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=F6R:FRUCTOSE+-6-PHOSPHATE'>F6R</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
<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'>[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'>[https://proteopedia.org/fgij/fg.htm?mol=3te9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3te9 OCA], [https://pdbe.org/3te9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3te9 RCSB], [https://www.ebi.ac.uk/pdbsum/3te9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3te9 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=3te9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3te9 OCA], [https://pdbe.org/3te9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3te9 RCSB], [https://www.ebi.ac.uk/pdbsum/3te9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3te9 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]  
[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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3te9" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Transaldolase 3D structures|Transaldolase 3D structures]]
*[[Transaldolase 3D structures|Transaldolase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Francisella tularensis subsp. nearctica olsufjev 1970]]
[[Category: Francisella tularensis subsp. tularensis]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Transaldolase]]
[[Category: Anderson WF]]
[[Category: Anderson, W F]]
[[Category: Halavaty A]]
[[Category: Structural genomic]]
[[Category: Light SH]]
[[Category: Halavaty, A]]
[[Category: Minasov G]]
[[Category: Light, S H]]
[[Category: Papazisi L]]
[[Category: Minasov, G]]
[[Category: Shuvalova L]]
[[Category: Papazisi, L]]
[[Category: Shuvalova, L]]
[[Category: Alpha-beta barrel/tim barrel]]
[[Category: Csgid]]
[[Category: Sedoheptulose-7-phosphate:d-glyceraldehyde-3-phosphate glyceronetransferase activity]]
[[Category: Transferase]]

Latest revision as of 16:25, 14 March 2024

1.8 Angstrom Resolution Crystal Structure of K135M Mutant of Transaldolase B (TalA) from Francisella tularensis in Complex with Fructose 6-phosphate1.8 Angstrom Resolution Crystal Structure of K135M Mutant of Transaldolase B (TalA) from Francisella tularensis in Complex with Fructose 6-phosphate

Structural highlights

3te9 is a 2 chain structure with sequence from Francisella tularensis subsp. tularensis. 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

3te9, resolution 1.80Å

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