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2f9t

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Revision as of 09:25, 14 June 2018

Structure of the type III CoaA from Pseudomonas aeruginosa

Structural highlights

2f9t is a 2 chain structure with sequence from Pseae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Related:	2f9w
Activity:	Pantothenate kinase, with EC number 2.7.1.33
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2f9t"

@@ Line 1: / Line 1: @@
 ==Structure of the type III CoaA from Pseudomonas aeruginosa==
 <StructureSection load='2f9t' size='340' side='right' caption='[[2f9t]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2f9w|2f9w]]</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='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]</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>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f9/2f9t_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f9/2f9t_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2f9t ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">

2f9t

From Proteopedia

Revision as of 09:25, 14 June 2018

Structure of the type III CoaA from Pseudomonas aeruginosa

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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