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==Crystal structure of S. aureus Homoserine Dehydrogenase at pH6.0== | ==Crystal structure of S. aureus Homoserine Dehydrogenase at pH6.0== | ||
<StructureSection load='4pg4' size='340' side='right' caption='[[4pg4]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='4pg4' size='340' side='right'caption='[[4pg4]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4pg4]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PG4 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[4pg4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_M1064 Staphylococcus aureus M1064]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PG4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PG4 FirstGlance]. <br> | ||
</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=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></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=4pg4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pg4 OCA], [https://pdbe.org/4pg4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pg4 RCSB], [https://www.ebi.ac.uk/pdbsum/4pg4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pg4 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A0M3KKV6_STAAU A0A0M3KKV6_STAAU] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Homoserine dehydrogenase (HSD) is an oxidoreductase in the aspartic acid pathway. This enzyme coordinates a critical branch point of the metabolic pathway that leads to the synthesis of bacterial cell-wall components such as L-lysine and m-DAP in addition to other amino acids such as L-threonine, L-methionine and L-isoleucine. Here, a structural rationale for the hydride-transfer step in the reaction mechanism of HSD is reported. The structure of Staphylococcus aureus HSD was determined at different pH conditions to understand the basis for the enhanced enzymatic activity at basic pH. An analysis of the crystal structure revealed that Lys105, which is located at the interface of the catalytic and cofactor-binding sites, could mediate the hydride-transfer step of the reaction mechanism. The role of Lys105 was subsequently confirmed by mutational analysis. Put together, these studies reveal the role of conserved water molecules and a lysine residue in hydride transfer between the substrate and the cofactor. | |||
Structural basis for the catalytic mechanism of homoserine dehydrogenase.,Navratna V, Reddy G, Gopal B Acta Crystallogr D Biol Crystallogr. 2015 May;71(Pt 5):1216-25. doi:, 10.1107/S1399004715004617. Epub 2015 Apr 30. PMID:25945586<ref>PMID:25945586</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4pg4" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Staphylococcus aureus M1064]] | ||
[[Category: | [[Category: Gopal B]] | ||
[[Category: | [[Category: Navratna V]] | ||
Latest revision as of 10:16, 27 September 2023
Crystal structure of S. aureus Homoserine Dehydrogenase at pH6.0Crystal structure of S. aureus Homoserine Dehydrogenase at pH6.0
Structural highlights
FunctionPublication Abstract from PubMedHomoserine dehydrogenase (HSD) is an oxidoreductase in the aspartic acid pathway. This enzyme coordinates a critical branch point of the metabolic pathway that leads to the synthesis of bacterial cell-wall components such as L-lysine and m-DAP in addition to other amino acids such as L-threonine, L-methionine and L-isoleucine. Here, a structural rationale for the hydride-transfer step in the reaction mechanism of HSD is reported. The structure of Staphylococcus aureus HSD was determined at different pH conditions to understand the basis for the enhanced enzymatic activity at basic pH. An analysis of the crystal structure revealed that Lys105, which is located at the interface of the catalytic and cofactor-binding sites, could mediate the hydride-transfer step of the reaction mechanism. The role of Lys105 was subsequently confirmed by mutational analysis. Put together, these studies reveal the role of conserved water molecules and a lysine residue in hydride transfer between the substrate and the cofactor. Structural basis for the catalytic mechanism of homoserine dehydrogenase.,Navratna V, Reddy G, Gopal B Acta Crystallogr D Biol Crystallogr. 2015 May;71(Pt 5):1216-25. doi:, 10.1107/S1399004715004617. Epub 2015 Apr 30. PMID:25945586[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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