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3myp

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Current revision (09:58, 14 February 2024) (edit) (undo)
 
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<StructureSection load='3myp' size='340' side='right'caption='[[3myp]], [[Resolution|resolution]] 2.99&Aring;' scene=''>
<StructureSection load='3myp' size='340' side='right'caption='[[3myp]], [[Resolution|resolution]] 2.99&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3myp]] is a 4 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=3MYP FirstGlance]. <br>
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<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>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.99&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3myo|3myo]]</div></td></tr>
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<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>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lacD, SACOL2183 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=93062 STAAC])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Tagatose-bisphosphate_aldolase Tagatose-bisphosphate aldolase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.40 4.1.2.40] </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=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='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>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/LACD_STAAC LACD_STAAC]
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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).
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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<ref>PMID:21192932</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3myp" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Aldolase 3D structures|Aldolase 3D structures]]
*[[Aldolase 3D structures|Aldolase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Staac]]
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[[Category: Staphylococcus aureus subsp. aureus COL]]
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[[Category: Tagatose-bisphosphate aldolase]]
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[[Category: Kim DJ]]
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[[Category: Kim, D J]]
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[[Category: Kim HS]]
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[[Category: Kim, H S]]
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[[Category: Kim KH]]
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[[Category: Kim, K H]]
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[[Category: Lee SJ]]
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[[Category: Lee, S J]]
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[[Category: Suh SW]]
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[[Category: Suh, S W]]
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[[Category: Yoon HJ]]
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[[Category: Yoon, H J]]
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[[Category: Yoon JY]]
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[[Category: Yoon, J Y]]
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[[Category: Beta-alpha-barrel]]
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[[Category: Lyase]]
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Current revision

Crystal structure of tagatose-1,6-bisphosphate aldolase from Staphylococcus aureus

PDB ID 3myp

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