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==Structure of the E. coli C-P lyase core complex==
==Structure of the E. coli C-P lyase core complex==
<StructureSection load='4xb6' size='340' side='right' caption='[[4xb6]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='4xb6' size='340' side='right'caption='[[4xb6]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4xb6]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XB6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XB6 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4xb6]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_str._K-12_substr._MG1655 Escherichia coli str. K-12 substr. MG1655]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XB6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XB6 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.7&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-D-ribose_1-methylphosphonate_5-triphosphate_synthase Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.8.37 2.7.8.37] </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=4xb6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xb6 OCA], [https://pdbe.org/4xb6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xb6 RCSB], [https://www.ebi.ac.uk/pdbsum/4xb6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xb6 ProSAT]</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=4xb6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xb6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4xb6 RCSB], [http://www.ebi.ac.uk/pdbsum/4xb6 PDBsum]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/PHNJ_ECOLI PHNJ_ECOLI]] Catalyzes the breakage of the C-P bond in alpha-D-ribose 1-methylphosphonate 5-phosphate (PRPn) forming alpha-D-ribose 1,2-cyclic phosphate 5-phosphate (PRcP).<ref>PMID:22089136</ref>  [[http://www.uniprot.org/uniprot/PHNG_ECOLI PHNG_ECOLI]] Together with PhnH, PhnI and PhnL is required for the transfer of the ribose triphosphate moiety from ATP to methyl phosphonate.<ref>PMID:22089136</ref> [[http://www.uniprot.org/uniprot/PHNI_ECOLI PHNI_ECOLI]] Together with PhnG, PhnH and PhnL is required for the transfer of the ribose triphosphate moiety from ATP to methyl phosphonate. PhnI alone has nucleosidase activity, catalyzing the hydrolysis of ATP or GTP forming alpha-D-ribose 5-triphosphate and adenine or guanine, respectively.<ref>PMID:22089136</ref>  [[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/PHNG_ECOLI PHNG_ECOLI] Together with PhnH, PhnI and PhnL is required for the transfer of the ribose triphosphate moiety from ATP to methyl phosphonate.<ref>PMID:22089136</ref>  
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 4xb6" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase]]
[[Category: Escherichia coli str. K-12 substr. MG1655]]
[[Category: Brodersen, D E]]
[[Category: Large Structures]]
[[Category: Protein complex]]
[[Category: Brodersen DE]]
[[Category: Transferase]]
Retrieved from "https://proteopedia.org/4xb6"