4nb4: Difference between revisions
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==Pantothenamide-bound Pantothenate kinase from Staphylococcus aureus== | |||
<StructureSection load='4nb4' size='340' side='right'caption='[[4nb4]], [[Resolution|resolution]] 2.25Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4nb4]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_MRSA252 Staphylococcus aureus subsp. aureus MRSA252]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NB4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NB4 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]] 2.25Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SH3:N-[2-(1,3-BENZODIOXOL-5-YL)ETHYL]-N~3~-[(2R)-2-HYDROXY-3,3-DIMETHYL-4-(PHOSPHONOOXY)BUTANOYL]-BETA-ALANINAMIDE'>SH3</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=4nb4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nb4 OCA], [https://pdbe.org/4nb4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nb4 RCSB], [https://www.ebi.ac.uk/pdbsum/4nb4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nb4 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/COAW_STAAS COAW_STAAS] Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.<ref>PMID:16905099</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Pantothenate kinase (PanK) is the rate-limiting enzyme in Coenzyme A biosynthesis, catalyzing the ATP-dependent phosphorylation of pantothenate. We solved the co-crystal structures of PanKs from Staphylococcus aureus (SaPanK) and Klebsiella pneumonia (KpPanK) with N-[2-(1,3-benzodioxol-5-yl)ethyl] pantothenamide (N354-Pan). Two different N354-Pan conformers interact with polar/nonpolar mixed residues in SaPanK and aromatic residues in KpPanK. Additionally, phosphorylated N354-Pan is found at the closed active site of SaPanK but not at the open active site of KpPanK, suggesting an exchange of the phosphorylated product with a new N354-Pan only in KpPanK. Together, pantothenamides conformational flexibility and binding pocket are two key considerations for selective compound design. Proteins 2014. (c) 2014 Wiley Periodicals, Inc. | |||
Structural characterization of a new N-substituted pantothenamide bound to pantothenate kinases from Klebsiella pneumonia and Staphylococcus aureus.,Hughes SJ, Antoshchenko T, Kim KP, Smil D, Park HW Proteins. 2014 Jan 28. doi: 10.1002/prot.24524. PMID:24470271<ref>PMID:24470271</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4nb4" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Pantothenate kinase 3D structures|Pantothenate kinase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Staphylococcus aureus subsp. aureus MRSA252]] | |||
[[Category: Antoshchenko T]] | |||
[[Category: Hughes SJ]] | |||
[[Category: Park HW]] | |||
[[Category: Smil D]] | |||
Latest revision as of 19:52, 20 September 2023
Pantothenamide-bound Pantothenate kinase from Staphylococcus aureusPantothenamide-bound Pantothenate kinase from Staphylococcus aureus
Structural highlights
FunctionCOAW_STAAS Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.[1] Publication Abstract from PubMedPantothenate kinase (PanK) is the rate-limiting enzyme in Coenzyme A biosynthesis, catalyzing the ATP-dependent phosphorylation of pantothenate. We solved the co-crystal structures of PanKs from Staphylococcus aureus (SaPanK) and Klebsiella pneumonia (KpPanK) with N-[2-(1,3-benzodioxol-5-yl)ethyl] pantothenamide (N354-Pan). Two different N354-Pan conformers interact with polar/nonpolar mixed residues in SaPanK and aromatic residues in KpPanK. Additionally, phosphorylated N354-Pan is found at the closed active site of SaPanK but not at the open active site of KpPanK, suggesting an exchange of the phosphorylated product with a new N354-Pan only in KpPanK. Together, pantothenamides conformational flexibility and binding pocket are two key considerations for selective compound design. Proteins 2014. (c) 2014 Wiley Periodicals, Inc. Structural characterization of a new N-substituted pantothenamide bound to pantothenate kinases from Klebsiella pneumonia and Staphylococcus aureus.,Hughes SJ, Antoshchenko T, Kim KP, Smil D, Park HW Proteins. 2014 Jan 28. doi: 10.1002/prot.24524. PMID:24470271[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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