4hmw: Difference between revisions

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'''Unreleased structure'''


The entry 4hmw is ON HOLD
==Crystal structure of PhzG from Burkholderia lata 383==
<StructureSection load='4hmw' size='340' side='right'caption='[[4hmw]], [[Resolution|resolution]] 1.53&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4hmw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_lata Burkholderia lata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HMW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HMW 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]] 1.53&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</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=4hmw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hmw OCA], [https://pdbe.org/4hmw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hmw RCSB], [https://www.ebi.ac.uk/pdbsum/4hmw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hmw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PHZG_BURL3 PHZG_BURL3] Involved in the biosynthesis of the antibiotic phenazine, a nitrogen-containing heterocyclic molecule having important roles in virulence, competition and biological control (PubMed:23897464). Catalyzes several oxidations in the terminal steps of core phenazine biosynthesis. It oxidizes both hexahydrophenazine-1,6-dicarboxylic acid (HHPDC) and tetrahydrophenazine-1-carboxylic acid (THPCA) and thereby contributes to the generation of both phenazine-1,6-dicarboxylic acid (PDC) and phenazine-1-carboxylic acid (PCA). It synthesizes phenazines in their reduced form, which are the likely end products in vivo (PubMed:23897464).<ref>PMID:23897464</ref>


Authors: Xu, N.N., Ahuja, E.G., Blankenfeldt, W.
==See Also==
 
*[[Pyridoxine 5'-phosphate oxidase|Pyridoxine 5'-phosphate oxidase]]
Description: Crystal structure of PhzG from Burkholderia lata 383
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Burkholderia lata]]
[[Category: Large Structures]]
[[Category: Ahuja EG]]
[[Category: Blankenfeldt W]]
[[Category: Xu NN]]

Latest revision as of 11:52, 20 March 2024

Crystal structure of PhzG from Burkholderia lata 383Crystal structure of PhzG from Burkholderia lata 383

Structural highlights

4hmw is a 2 chain structure with sequence from Burkholderia lata. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.53Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PHZG_BURL3 Involved in the biosynthesis of the antibiotic phenazine, a nitrogen-containing heterocyclic molecule having important roles in virulence, competition and biological control (PubMed:23897464). Catalyzes several oxidations in the terminal steps of core phenazine biosynthesis. It oxidizes both hexahydrophenazine-1,6-dicarboxylic acid (HHPDC) and tetrahydrophenazine-1-carboxylic acid (THPCA) and thereby contributes to the generation of both phenazine-1,6-dicarboxylic acid (PDC) and phenazine-1-carboxylic acid (PCA). It synthesizes phenazines in their reduced form, which are the likely end products in vivo (PubMed:23897464).[1]

See Also

References

  1. Xu N, Ahuja EG, Janning P, Mavrodi DV, Thomashow LS, Blankenfeldt W. Trapped intermediates in crystals of the FMN-dependent oxidase PhzG provide insight into the final steps of phenazine biosynthesis. Acta Crystallogr D Biol Crystallogr. 2013 Aug;69(Pt 8):1403-13. doi:, 10.1107/S0907444913008354. Epub 2013 Jul 13. PMID:23897464 doi:http://dx.doi.org/10.1107/S0907444913008354

4hmw, resolution 1.53Å

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