4e0c
From Proteopedia
(Difference between revisions)
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== 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 [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> | ||
| - | </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>< | + | </td></tr><tr id='ligand'><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></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='related'><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><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=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://www.rcsb.org/pdb/explore.do?structureId=4e0c RCSB], [http://www.ebi.ac.uk/pdbsum/4e0c 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 == | ||
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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/> | ||
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[[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: National institute of allergy and infectious disease]] | [[Category: National institute of allergy and infectious disease]] | ||
[[Category: Niaid]] | [[Category: Niaid]] | ||
| - | [[Category: Structural genomic]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 02:33, 25 December 2014
1.8 Angstrom Resolution Crystal Structure of Transaldolase from Francisella tularensis (phosphate-free)
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