5eqn: Difference between revisions

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'''Unreleased structure'''


The entry 5eqn is ON HOLD  until Paper Publication
==Structure of phosphonate hydroxylase==
<StructureSection load='5eqn' size='340' side='right' caption='[[5eqn]], [[Resolution|resolution]] 2.30&Aring;' 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.


Authors: Li, C., Hu, Y., Zhang, H.
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>


Description: Structure of phosphonate hydroxylase
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 5eqn" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Hu, Y]]
[[Category: Li, C]]
[[Category: Zhang, H]]
[[Category: Zhang, H]]
[[Category: Li, C]]
[[Category: Dioxygenase]]
[[Category: Hu, Y]]
[[Category: Hydrolase]]
[[Category: Phosphonate hydroxylase]]
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