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| | <StructureSection load='2f9t' size='340' side='right'caption='[[2f9t]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='2f9t' size='340' side='right'caption='[[2f9t]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2f9t]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseae Pseae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F9T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2F9T FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2f9t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseae Pseae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F9T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F9T FirstGlance]. <br> |
| | </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> | | </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> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2f9w|2f9w]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2f9w|2f9w]]</div></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pantothenate_kinase Pantothenate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.33 2.7.1.33] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Pantothenate_kinase Pantothenate kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.33 2.7.1.33] </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=2f9t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f9t OCA], [http://pdbe.org/2f9t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2f9t RCSB], [http://www.ebi.ac.uk/pdbsum/2f9t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2f9t 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=2f9t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f9t OCA], [https://pdbe.org/2f9t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f9t RCSB], [https://www.ebi.ac.uk/pdbsum/2f9t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f9t ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/COAX_PSEAE COAX_PSEAE]] Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis. Can utilize a wide range of phosphoryl donors other than ATP, and does not discriminate between purine- and pyrimidine-based nucleotides or deoxynucleotides. Is responsible for the resistance of P.aeruginosa to the pantothenamide antibiotics, since it can not bind and phosphorylate these pantothenate analogs.<ref>PMID:16905099</ref> | + | [[https://www.uniprot.org/uniprot/COAX_PSEAE COAX_PSEAE]] Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis. Can utilize a wide range of phosphoryl donors other than ATP, and does not discriminate between purine- and pyrimidine-based nucleotides or deoxynucleotides. Is responsible for the resistance of P.aeruginosa to the pantothenamide antibiotics, since it can not bind and phosphorylate these pantothenate analogs.<ref>PMID:16905099</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Structural highlights
Function
[COAX_PSEAE] Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis. Can utilize a wide range of phosphoryl donors other than ATP, and does not discriminate between purine- and pyrimidine-based nucleotides or deoxynucleotides. Is responsible for the resistance of P.aeruginosa to the pantothenamide antibiotics, since it can not bind and phosphorylate these pantothenate analogs.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Three distinct isoforms of pantothenate kinase (CoaA) in bacteria catalyze the first step in coenzyme A biosynthesis. The structures of the type II (Staphylococcus aureus, SaCoaA) and type III (Pseudomonas aeruginosa, PaCoaA) enzymes reveal that they assemble nearly identical subunits with actin-like folds into dimers that exhibit distinct biochemical properties. PaCoaA has a fully enclosed pantothenate binding pocket and requires a monovalent cation to weakly bind ATP in an open cavity that does not interact with the adenine nucleotide. Pantothenate binds to an open pocket in SaCoaA that strongly binds ATP by using a classical P loop architecture coupled with specific interactions with the adenine moiety. The PaCoaA*Pan binary complex explains the resistance of bacteria possessing this isoform to the pantothenamide antibiotics, and the similarity between SaCoaA and human pantothenate kinase 2 explains the molecular basis for the development of the neurodegenerative phenotype in three mutations in the human protein.
Prokaryotic type II and type III pantothenate kinases: The same monomer fold creates dimers with distinct catalytic properties.,Hong BS, Yun MK, Zhang YM, Chohnan S, Rock CO, White SW, Jackowski S, Park HW, Leonardi R Structure. 2006 Aug;14(8):1251-61. PMID:16905099[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hong BS, Yun MK, Zhang YM, Chohnan S, Rock CO, White SW, Jackowski S, Park HW, Leonardi R. Prokaryotic type II and type III pantothenate kinases: The same monomer fold creates dimers with distinct catalytic properties. Structure. 2006 Aug;14(8):1251-61. PMID:16905099 doi:10.1016/j.str.2006.06.008
- ↑ Hong BS, Yun MK, Zhang YM, Chohnan S, Rock CO, White SW, Jackowski S, Park HW, Leonardi R. Prokaryotic type II and type III pantothenate kinases: The same monomer fold creates dimers with distinct catalytic properties. Structure. 2006 Aug;14(8):1251-61. PMID:16905099 doi:10.1016/j.str.2006.06.008
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