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| | <StructureSection load='2fsu' size='340' side='right'caption='[[2fsu]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='2fsu' size='340' side='right'caption='[[2fsu]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2fsu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FSU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FSU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2fsu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FSU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FSU FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</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='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=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=2fsu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fsu OCA], [http://pdbe.org/2fsu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fsu RCSB], [http://www.ebi.ac.uk/pdbsum/2fsu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2fsu ProSAT], [http://www.topsan.org/Proteins/BSGI/2fsu TOPSAN]</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=2fsu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fsu OCA], [https://pdbe.org/2fsu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fsu RCSB], [https://www.ebi.ac.uk/pdbsum/2fsu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fsu ProSAT], [https://www.topsan.org/Proteins/BSGI/2fsu TOPSAN]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PHNH_ECOLI PHNH_ECOLI]] Together with PhnG, PhnI and PhnL is required for the transfer of the ribose triphosphate moiety from ATP to methyl phosphonate.<ref>PMID:22089136</ref> | + | [https://www.uniprot.org/uniprot/PHNH_ECOLI PHNH_ECOLI] Together with PhnG, PhnI and PhnL is required for the transfer of the ribose triphosphate moiety from ATP to methyl phosphonate.<ref>PMID:22089136</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fs/2fsu_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fs/2fsu_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | [[Category: Escherichia coli]] | | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Adams, M A]] | + | [[Category: Adams MA]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Jia Z]] |
| - | [[Category: Jia, Z]] | + | [[Category: Luo Y]] |
| - | [[Category: Luo, Y]] | + | [[Category: Zechel DL]] |
| - | [[Category: Zechel, D L]] | + | |
| - | [[Category: Bsgi]]
| + | |
| - | [[Category: C-p lyase]]
| + | |
| - | [[Category: Phnh]]
| + | |
| - | [[Category: Phosphonate metabolism]]
| + | |
| - | [[Category: Unknown function]]
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| Structural highlights
Function
PHNH_ECOLI Together with PhnG, PhnI and PhnL is required for the transfer of the ribose triphosphate moiety from ATP to methyl phosphonate.[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
Organophosphonates are reduced forms of phosphorous that are characterized by the presence of a stable carbon-phosphorus (C-P) bond, which resists chemical hydrolysis, thermal decomposition, and photolysis. The chemically inert nature of the C-P bond has raised environmental concerns as toxic phosphonates accumulate in a number of ecosystems. Carbon-phosphorous lyase (CP lyase) is a multienzyme pathway encoded by the phn operon in gram-negative bacteria. In Escherichia coli 14 cistrons comprise the operon (phnCDEFGHIJKLMNOP) and collectively allow the internalization and degradation of phosphonates. Here we report the X-ray crystal structure of the PhnH component at 1.77 A resolution. The protein exhibits a novel fold, although local similarities with the pyridoxal 5'-phosphate-dependent transferase family of proteins are apparent. PhnH forms a dimer in solution and in the crystal structure, the interface of which is implicated in creating a potential ligand binding pocket. Our studies further suggest that PhnH may be capable of binding negatively charged cyclic compounds through interaction with strictly conserved residues. Finally, we show that PhnH is essential for C-P bond cleavage in the CP lyase pathway.
Crystal structure of PhnH: an essential component of carbon-phosphorus lyase in Escherichia coli.,Adams MA, Luo Y, Hove-Jensen B, He SM, van Staalduinen LM, Zechel DL, Jia Z J Bacteriol. 2008 Feb;190(3):1072-83. Epub 2007 Nov 9. PMID:17993513[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kamat SS, Williams HJ, Raushel FM. Intermediates in the transformation of phosphonates to phosphate by bacteria. Nature. 2011 Nov 16;480(7378):570-3. doi: 10.1038/nature10622. PMID:22089136 doi:http://dx.doi.org/10.1038/nature10622
- ↑ Adams MA, Luo Y, Hove-Jensen B, He SM, van Staalduinen LM, Zechel DL, Jia Z. Crystal structure of PhnH: an essential component of carbon-phosphorus lyase in Escherichia coli. J Bacteriol. 2008 Feb;190(3):1072-83. Epub 2007 Nov 9. PMID:17993513 doi:10.1128/JB.01274-07
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