6fux: Difference between revisions
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<StructureSection load='6fux' size='340' side='right'caption='[[6fux]], [[Resolution|resolution]] 1.65Å' scene=''> | <StructureSection load='6fux' size='340' side='right'caption='[[6fux]], [[Resolution|resolution]] 1.65Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6fux]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FUX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FUX FirstGlance]. <br> | <table><tr><td colspan='2'>[[6fux]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Strr1 Strr1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FUX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FUX FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SRY:STREPTOMYCIN'>SRY</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SRY:STREPTOMYCIN'>SRY</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6fuc|6fuc]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6fuc|6fuc]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SRIM_08058 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1265868 STRR1])</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=6fux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fux OCA], [http://pdbe.org/6fux PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fux RCSB], [http://www.ebi.ac.uk/pdbsum/6fux PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fux 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=6fux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fux OCA], [http://pdbe.org/6fux PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fux RCSB], [http://www.ebi.ac.uk/pdbsum/6fux PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fux ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In this study, we identified a new gene (aph(3'')-Id) coding for a streptomycin phosphotransferase by using phylogenetic comparative analysis of the genome of the oxytetracycline-producing strain Streptomyces rimosus ATCC 10970. Cloning the aph(3'')-Id gene in E.coli and inducing its expression led to an increase in the minimum inhibitory concentration of the recombinant E.coli strain to streptomycin reaching 350mug/ml. To evaluate the phosphotransferase activity of the recombinant protein APH(3'')-Id we carried out thin-layer chromatography of the putative (32)P-labeled streptomycin phosphate. We also performed a spectrophotometric analysis to determine the production of ADP coupled to NADH oxidation. Here are the kinetic parameters of the streptomycin phosphotransferase APH(3'')-Id: Km 80.4muM, Vmax 6.45mumol/min/mg and kcat 1.73 s(-1). We demonstrated for the first time the ability of the aminoglycoside phototransferase (APH(3'')-Id) to undergo autophosphorylation in vitro. The 3D structures of APH(3'')-Id in its unliganded state and in ternary complex with streptomycin and ADP were obtained. The structure of the ternary complex is the first example of this class of enzymes with bound streptomycin. Comparison of the obtained structures with those of other aminoglycoside phosphotransferases revealed peculiar structure of the substrate-binding pocket reflecting its specificity to a particular antibiotic. | |||
Identification, functional and structural characterization of novel aminoglycoside phosphotransferase APH(3'')-Id from Streptomyces rimosus subsp. rimosus ATCC 10970.,Alekseeva MG, Boyko KM, Nikolaeva AY, Mavletova DA, Rudakova NN, Zakharevich NV, Korzhenevskiy DA, Ziganshin RH, Popov VO, Danilenko VN Arch Biochem Biophys. 2019 Jun 26;671:111-122. doi: 10.1016/j.abb.2019.06.008. PMID:31251922<ref>PMID:31251922</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6fux" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Strr1]] | |||
[[Category: Alekseeva, M G]] | [[Category: Alekseeva, M G]] | ||
[[Category: Boyko, K M]] | [[Category: Boyko, K M]] |