This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
3tno
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3tno]] 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=3TNO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TNO FirstGlance]. <br> | <table><tr><td colspan='2'>[[3tno]] 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=3TNO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TNO FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=I22:D-ALTRO-HEPT-2-ULOSE+7-PHOSPHATE'>I22</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=I22:D-ALTRO-HEPT-2-ULOSE+7-PHOSPHATE'>I22</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3igx|3igx]], [[3tk7|3tk7]], [[3tkf|3tkf]], [[3te9|3te9]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3igx|3igx]], [[3tk7|3tk7]], [[3tkf|3tkf]], [[3te9|3te9]]</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='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><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3tno FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tno OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tno RCSB], [http://www.ebi.ac.uk/pdbsum/3tno 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=3tno FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tno OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tno RCSB], [http://www.ebi.ac.uk/pdbsum/3tno PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://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 15: | Line 17: | ||
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> | 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 | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
</div> | </div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Transaldolase|Transaldolase]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 23: | Line 28: | ||
[[Category: Fratt]] | [[Category: Fratt]] | ||
[[Category: Transaldolase]] | [[Category: Transaldolase]] | ||
| - | [[Category: Anderson, W F | + | [[Category: Anderson, W F]] |
| - | [[Category: | + | [[Category: Structural genomic]] |
| - | [[Category: Halavaty, A S | + | [[Category: Halavaty, A S]] |
| - | [[Category: Light, S H | + | [[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: Alpha-beta barrel/tim barrel]] | ||
| - | [[Category: Center for structural genomics of infectious disease]] | ||
[[Category: Csgid]] | [[Category: Csgid]] | ||
| - | [[Category: Structural genomic]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 01:38, 25 December 2014
1.65 Angstrom Resolution Crystal Structure of Transaldolase B (TalA) from Francisella tularensis in Covalent Complex with Sedoheptulose-7-Phosphate
| |||||||||||
