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==Pseudomonas fluorescens PhoX in complex with the substrate analogue AppCp== | ==Pseudomonas fluorescens PhoX in complex with the substrate analogue AppCp== | ||
<StructureSection load='4amf' size='340' side='right' caption='[[4amf]], [[Resolution|resolution]] 1.52Å' scene=''> | <StructureSection load='4amf' size='340' side='right'caption='[[4amf]], [[Resolution|resolution]] 1.52Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4amf]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4amf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_fluorescens_Pf0-1 Pseudomonas fluorescens Pf0-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AMF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AMF FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FEO:MU-OXO-DIIRON'>FEO</scene>, <scene name='pdbligand=LI:LITHIUM+ION'>LI</scene | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.52Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FEO:MU-OXO-DIIRON'>FEO</scene>, <scene name='pdbligand=LI:LITHIUM+ION'>LI</scene></td></tr> | |||
<tr | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4amf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4amf OCA], [https://pdbe.org/4amf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4amf RCSB], [https://www.ebi.ac.uk/pdbsum/4amf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4amf ProSAT]</span></td></tr> | ||
</table> | |||
<table> | == Function == | ||
[https://www.uniprot.org/uniprot/Q3K5N8_PSEPF Q3K5N8_PSEPF] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Alkaline phosphatases play a crucial role in phosphate acquisition by microorganisms. To expand our understanding of catalysis by this class of enzymes, we have determined the structure of the widely occurring microbial alkaline phosphatase PhoX. The enzyme contains a complex active-site cofactor comprising two antiferromagnetically coupled ferric iron ions (Fe(3+)), three calcium ions (Ca(2+)), and an oxo group bridging three of the metal ions. Notably, the main part of the cofactor resembles synthetic oxide-centered triangular metal complexes. Structures of PhoX-ligand complexes reveal how the active-site metal ions bind substrate and implicate the cofactor oxo group in the catalytic mechanism. The presence of iron in PhoX raises the possibility that iron bioavailability limits microbial phosphate acquisition. | |||
A complex iron-calcium cofactor catalyzing phosphotransfer chemistry.,Yong SC, Roversi P, Lillington J, Rodriguez F, Krehenbrink M, Zeldin OB, Garman EF, Lea SM, Berks BC Science. 2014 Sep 5;345(6201):1170-3. doi: 10.1126/science.1254237. PMID:25190793<ref>PMID:25190793</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4amf" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Pseudomonas fluorescens Pf0-1]] | ||
[[Category: Berks | [[Category: Berks BC]] | ||
[[Category: Garman | [[Category: Garman EF]] | ||
[[Category: Lea | [[Category: Lea SM]] | ||
[[Category: Lillington | [[Category: Lillington JED]] | ||
[[Category: Roversi | [[Category: Roversi P]] | ||
[[Category: Yong | [[Category: Yong SC]] | ||
[[Category: Zeldin | [[Category: Zeldin OB]] | ||
Latest revision as of 14:30, 20 December 2023
Pseudomonas fluorescens PhoX in complex with the substrate analogue AppCpPseudomonas fluorescens PhoX in complex with the substrate analogue AppCp
Structural highlights
FunctionPublication Abstract from PubMedAlkaline phosphatases play a crucial role in phosphate acquisition by microorganisms. To expand our understanding of catalysis by this class of enzymes, we have determined the structure of the widely occurring microbial alkaline phosphatase PhoX. The enzyme contains a complex active-site cofactor comprising two antiferromagnetically coupled ferric iron ions (Fe(3+)), three calcium ions (Ca(2+)), and an oxo group bridging three of the metal ions. Notably, the main part of the cofactor resembles synthetic oxide-centered triangular metal complexes. Structures of PhoX-ligand complexes reveal how the active-site metal ions bind substrate and implicate the cofactor oxo group in the catalytic mechanism. The presence of iron in PhoX raises the possibility that iron bioavailability limits microbial phosphate acquisition. A complex iron-calcium cofactor catalyzing phosphotransfer chemistry.,Yong SC, Roversi P, Lillington J, Rodriguez F, Krehenbrink M, Zeldin OB, Garman EF, Lea SM, Berks BC Science. 2014 Sep 5;345(6201):1170-3. doi: 10.1126/science.1254237. PMID:25190793[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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