5eqn
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of phosphonate hydroxylase== | |
| + | <StructureSection load='5eqn' size='340' side='right'caption='[[5eqn]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5eqn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_rubellomurinus Streptomyces rubellomurinus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EQN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EQN FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=5eqn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5eqn OCA], [https://pdbe.org/5eqn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5eqn RCSB], [https://www.ebi.ac.uk/pdbsum/5eqn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5eqn ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/FRBJ_STRR3 FRBJ_STRR3] Monooxygenase involved in the biosynthesis of the phosphonate antibiotic FR-33289, an antimalarial agent (PubMed:20142041). Catalyzes the oxidative decarboxylation of the antibiotic FR-900098 (3-(N-acetyl-N-hydroxy)aminopropylphosphonate) to form FR-33289 ((R)-(3-(acetylhydroxyamino)-2-hydroxypropyl)phosphonate) (PubMed:20142041).<ref>PMID:20142041</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | FrbJ is a member of the Fe(2+)/alpha-ketoglutarate-dependent dioxygenase family which hydroxylates the natural product FR-900098 of Streptomyces rubellomurinus, yielding the phosphonate antibiotic FR-33289. Here, the crystal structure of FrbJ, which shows structural homology to taurine dioxygenase (TauD), a key member of the same family, is reported. Unlike other members of the family, FrbJ has an unusual lid structure which consists of two beta-strands with a long loop between them. To investigate the role of this lid motif, a molecular-dynamics simulation was performed with the FrbJ structure. The molecular-dynamics simulation analysis implies that the lid-loop region is highly flexible, which is consistent with the fact that FrbJ has a relatively broad spectrum of substrates with different lengths. Interestingly, an access tunnel is found at the back of the active site which connects the putative binding site of alpha-ketoglutarate to the solvent outside. | ||
| - | + | Structural analysis of a phosphonate hydroxylase with an access tunnel at the back of the active site.,Li C, Junaid M, Almuqri EA, Hao S, Zhang H Acta Crystallogr F Struct Biol Commun. 2016 May 1;72(Pt 5):362-8. doi:, 10.1107/S2053230X16004933. Epub 2016 Apr 22. PMID:27139827<ref>PMID:27139827</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 5eqn" style="background-color:#fffaf0;"></div> |
| - | [[Category: Li | + | == References == |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Streptomyces rubellomurinus]] | ||
| + | [[Category: Hu Y]] | ||
| + | [[Category: Li C]] | ||
| + | [[Category: Zhang H]] | ||
Current revision
Structure of phosphonate hydroxylase
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