5eqn
From Proteopedia
(Difference between revisions)
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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. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5EQN FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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='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=5eqn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5eqn OCA], [http://pdbe.org/5eqn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5eqn RCSB], [http://www.ebi.ac.uk/pdbsum/5eqn PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <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> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5eqn" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Hu, Y]] | [[Category: Hu, Y]] | ||
| + | [[Category: Li, C]] | ||
| + | [[Category: Zhang, H]] | ||
| + | [[Category: Dioxygenase]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Phosphonate hydroxylase]] | ||
Revision as of 15:52, 1 June 2016
Structure of phosphonate hydroxylase
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