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| | <StructureSection load='3r5e' size='340' side='right'caption='[[3r5e]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='3r5e' size='340' side='right'caption='[[3r5e]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3r5e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"micrococcus_glutamicus"_kinoshita_et_al._1958 "micrococcus glutamicus" kinoshita et al. 1958]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R5E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3R5E FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3r5e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_glutamicum Corynebacterium glutamicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R5E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3R5E FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.1Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3r8r|3r8r]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cg1776, Cgl1575, tal ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1718 "Micrococcus glutamicus" Kinoshita et al. 1958])</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>
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| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3r5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r5e OCA], [https://pdbe.org/3r5e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3r5e RCSB], [https://www.ebi.ac.uk/pdbsum/3r5e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3r5e 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=3r5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r5e OCA], [https://pdbe.org/3r5e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3r5e RCSB], [https://www.ebi.ac.uk/pdbsum/3r5e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3r5e ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/Q8NQ64_CORGL Q8NQ64_CORGL]] Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway (By similarity).[HAMAP-Rule:MF_00493]
| + | [https://www.uniprot.org/uniprot/Q8NQ64_CORGL Q8NQ64_CORGL] Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway (By similarity).[HAMAP-Rule:MF_00493] |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
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| - | Transaldolase (Tal) is involved in the central carbon metabolism, i.e. the non-oxidative pentose phosphate pathway, and is therefore a ubiquitous enzyme. However, Tals show a low degree in sequence identity and vary in length within the enzyme family which previously led to the definition of five subfamilies. We wondered how this variation is conserved in structure and function. To answer this question we characterised and compared the Tals from Bacillus subtilis, Corynebacterium glutamicum and Escherichia coli, each belonging to a different subfamily, with respect to their biochemical properties and structures. The overall structure of the Tal domain, a (beta/alpha)(8) -barrel fold, is well conserved between the different subfamilies but the enzymes show different degrees of oligomerisation (monomer, dimer and decamer). The substrate specificity of the three enzymes investigated is quite similar which is reflected in the conservation of the active site, the phosphate binding site as well as the position of a catalytically important water molecule. All decameric enzymes characterised so far appear to be heat stable no matter whether they originate from a mesophilic or thermophilic organism. Hence, the thermostability might be due to the structural properties, i.e. tight packing, of these enzymes. Database The crystal structures have been deposited in the Protein Data Bank with accession code 3R8R for BsTal and 3R5E for CgTal. Structured digital abstract * BsTal and BsTal bind by x-ray crystallography (View interaction) * BsTal and BsTal bind by x-ray crystallography (View interaction).
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| - | Conservation of structure and mechanism within the transaldolase enzyme family.,Samland AK, Baier S, Schurmann M, Inoue T, Huf S, Schneider G, Sprenger GA, Sandalova T FEBS J. 2011 Dec 25. doi: 10.1111/j.1742-4658.2011.08467.x. PMID:22212631<ref>PMID:22212631</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
| + | |
| - | <div class="pdbe-citations 3r5e" style="background-color:#fffaf0;"></div>
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| | | | |
| | ==See Also== | | ==See Also== |
| | *[[Transaldolase 3D structures|Transaldolase 3D structures]] | | *[[Transaldolase 3D structures|Transaldolase 3D structures]] |
| - | == References == | |
| - | <references/> | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Micrococcus glutamicus kinoshita et al. 1958]] | + | [[Category: Corynebacterium glutamicum]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Transaldolase]]
| + | [[Category: Samland AK]] |
| - | [[Category: Samland, A K]] | + | [[Category: Sandalova T]] |
| - | [[Category: Sandalova, T]] | + | [[Category: Schneider G]] |
| - | [[Category: Schneider, G]] | + | |
| - | [[Category: Pentose phosphate pathway]]
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| - | [[Category: Tim barrel fold]]
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| - | [[Category: Transferase]]
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