3qy9: Difference between revisions
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< | ==The Crystal Structure of Dihydrodipicolinate reductase from Staphylococcus aureus== | ||
<StructureSection load='3qy9' size='340' side='right'caption='[[3qy9]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3qy9]] 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=3QY9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QY9 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=3qy9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qy9 OCA], [https://pdbe.org/3qy9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qy9 RCSB], [https://www.ebi.ac.uk/pdbsum/3qy9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qy9 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/DAPB_STAAC DAPB_STAAC] Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.[HAMAP-Rule:MF_00102] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Lysine biosynthesis proceeds by the nucleotide-dependent reduction of dihydrodipicolinate (DHDP) to tetrahydrodipicolinate (THDP) by dihydrodipicolinate reductase (DHDPR). The S. aureus DHDPR structure reveals different conformational states of this enzyme even in the absence of a substrate or nucleotide-cofactor. Despite lacking a conserved basic residue essential for NADPH interaction, S. aureus DHDPR differs from other homologues as NADPH is a more preferred co-factor than NADH. The structure provides a rationale-Lys35 compensates for the co-factor site mutation. These observations are significant for bi-ligand inhibitor design that relies on ligand-induced conformational changes as well as co-factor specificity for this important drug target. STRUCTURED SUMMARY OF PROTEIN INTERACTIONS: DHDPRbindstoDHDPR by molecular sieving(View interaction). DHDPRbindstoDHDPR by dynamic light scattering(View interaction). DHDPRbindstoDHDPR by X-ray crystallography(View interaction). | |||
Structure and nucleotide specificity of Staphylococcus aureus dihydrodipicolinate reductase (DapB).,Girish TS, Navratna V, Gopal B FEBS Lett. 2011 Aug 19;585(16):2561-7. Epub 2011 Jul 26. PMID:21803042<ref>PMID:21803042</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
== | </div> | ||
<div class="pdbe-citations 3qy9" style="background-color:#fffaf0;"></div> | |||
[[Category: | == References == | ||
[[Category: Staphylococcus aureus]] | <references/> | ||
[[Category: Girish | __TOC__ | ||
[[Category: Gopal | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Staphylococcus aureus subsp. aureus COL]] | |||
[[Category: Girish TS]] | |||
[[Category: Gopal B]] | |||
Latest revision as of 20:15, 1 November 2023
The Crystal Structure of Dihydrodipicolinate reductase from Staphylococcus aureusThe Crystal Structure of Dihydrodipicolinate reductase from Staphylococcus aureus
Structural highlights
FunctionDAPB_STAAC Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.[HAMAP-Rule:MF_00102] Publication Abstract from PubMedLysine biosynthesis proceeds by the nucleotide-dependent reduction of dihydrodipicolinate (DHDP) to tetrahydrodipicolinate (THDP) by dihydrodipicolinate reductase (DHDPR). The S. aureus DHDPR structure reveals different conformational states of this enzyme even in the absence of a substrate or nucleotide-cofactor. Despite lacking a conserved basic residue essential for NADPH interaction, S. aureus DHDPR differs from other homologues as NADPH is a more preferred co-factor than NADH. The structure provides a rationale-Lys35 compensates for the co-factor site mutation. These observations are significant for bi-ligand inhibitor design that relies on ligand-induced conformational changes as well as co-factor specificity for this important drug target. STRUCTURED SUMMARY OF PROTEIN INTERACTIONS: DHDPRbindstoDHDPR by molecular sieving(View interaction). DHDPRbindstoDHDPR by dynamic light scattering(View interaction). DHDPRbindstoDHDPR by X-ray crystallography(View interaction). Structure and nucleotide specificity of Staphylococcus aureus dihydrodipicolinate reductase (DapB).,Girish TS, Navratna V, Gopal B FEBS Lett. 2011 Aug 19;585(16):2561-7. Epub 2011 Jul 26. PMID:21803042[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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