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| | ==Crystal structure of tagatose-1,6-bisphosphate aldolase from Staphylococcus aureus== | | ==Crystal structure of tagatose-1,6-bisphosphate aldolase from Staphylococcus aureus== |
| - | <StructureSection load='3myp' size='340' side='right' caption='[[3myp]], [[Resolution|resolution]] 2.99Å' scene=''> | + | <StructureSection load='3myp' size='340' side='right'caption='[[3myp]], [[Resolution|resolution]] 2.99Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3myp]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Staac Staac]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MYP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MYP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3myp]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_COL Staphylococcus aureus subsp. aureus COL]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MYP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MYP FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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]] 2.99Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3myo|3myo]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lacD, SACOL2183 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=93062 STAAC])</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=3myp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3myp OCA], [https://pdbe.org/3myp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3myp RCSB], [https://www.ebi.ac.uk/pdbsum/3myp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3myp ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tagatose-bisphosphate_aldolase Tagatose-bisphosphate aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.40 4.1.2.40] </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=3myp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3myp OCA], [http://pdbe.org/3myp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3myp RCSB], [http://www.ebi.ac.uk/pdbsum/3myp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3myp ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/LACD_STAAC LACD_STAAC] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Aldolase|Aldolase]] | + | *[[Aldolase 3D structures|Aldolase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Staac]] | + | [[Category: Large Structures]] |
| - | [[Category: Tagatose-bisphosphate aldolase]] | + | [[Category: Staphylococcus aureus subsp. aureus COL]] |
| - | [[Category: Kim, D J]] | + | [[Category: Kim DJ]] |
| - | [[Category: Kim, H S]] | + | [[Category: Kim HS]] |
| - | [[Category: Kim, K H]] | + | [[Category: Kim KH]] |
| - | [[Category: Lee, S J]] | + | [[Category: Lee SJ]] |
| - | [[Category: Suh, S W]] | + | [[Category: Suh SW]] |
| - | [[Category: Yoon, H J]] | + | [[Category: Yoon HJ]] |
| - | [[Category: Yoon, J Y]] | + | [[Category: Yoon JY]] |
| - | [[Category: Beta-alpha-barrel]]
| + | |
| - | [[Category: Lyase]]
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| Structural highlights
Function
LACD_STAAC
Publication Abstract from PubMed
Staphylococcus aureus LacD, a Class I tagatose-1,6-bisphosphate (TBP) aldolase, shows broadened substrate specificity by catalyzing the cleavage of 1,6-bisphosphate derivatives of d-tagatose, d-fructose, d-sorbose, and d-psicose. LacD.1 and LacD.2 are two closely-related Class I TBP aldolases in Streptococcus pyogenes. Here we have determined the crystal structures of S. aureus LacD and S. pyogenes LacD.1. Monomers of both enzymes are folded into a (beta/alpha)(8) barrel and two monomers associate tightly to form a dimer in the crystals. The structures suggest that the residues E189 and S300 of rabbit muscle Class I fructose-1,6-bisphosphate (FBP) aldolase are important for substrate specificity. When we mutated the corresponding residues of S. aureus LacD, the mutants (L165E, L275S, and L165E/L275S) showed enhanced substrate specificity toward FBP. STRUCTURED SUMMARY: lacDbinds to lacD by X-ray crystallography(View interaction) lacD1binds to lacD1 by X-ray crystallography(View interaction).
Crystal structures of LacD from Staphylococcus aureus and LacD.1 from Streptococcus pyogenes: Insights into substrate specificity and virulence gene regulation.,Lee SJ, Kim HS, Kim do J, Yoon HJ, Kim KH, Yoon JY, Suh SW FEBS Lett. 2011 Jan 21;585(2):307-12. Epub 2010 Dec 28. PMID:21192932[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lee SJ, Kim HS, Kim do J, Yoon HJ, Kim KH, Yoon JY, Suh SW. Crystal structures of LacD from Staphylococcus aureus and LacD.1 from Streptococcus pyogenes: Insights into substrate specificity and virulence gene regulation. FEBS Lett. 2011 Jan 21;585(2):307-12. Epub 2010 Dec 28. PMID:21192932 doi:10.1016/j.febslet.2010.12.038
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