4pg7: Difference between revisions
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==Crystal structure of S. aureus Homoserine Dehydrogenase at pH7.5== | ==Crystal structure of S. aureus Homoserine Dehydrogenase at pH7.5== | ||
<StructureSection load='4pg7' size='340' side='right' caption='[[4pg7]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='4pg7' size='340' side='right' caption='[[4pg7]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4pg4|4pg4]], [[4pg5|4pg5]], [[4pg6|4pg6]], [[4pg8|4pg8]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4pg4|4pg4]], [[4pg5|4pg5]], [[4pg6|4pg6]], [[4pg8|4pg8]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Homoserine_dehydrogenase Homoserine dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.3 1.1.1.3] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Homoserine_dehydrogenase Homoserine dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.3 1.1.1.3] </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=4pg7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pg7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pg7 RCSB], [http://www.ebi.ac.uk/pdbsum/4pg7 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=4pg7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pg7 OCA], [http://pdbe.org/4pg7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pg7 RCSB], [http://www.ebi.ac.uk/pdbsum/4pg7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pg7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4pg7" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 15:12, 12 April 2017
Crystal structure of S. aureus Homoserine Dehydrogenase at pH7.5Crystal structure of S. aureus Homoserine Dehydrogenase at pH7.5
Structural highlights
Publication 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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