View source for 8i82


==Crystal structure of Cph001-D189N in complex with CMN IIA==
<StructureSection load='8i82' size='340' side='right'caption='[[8i82]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8i82]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharothrix_mutabilis_subsp._capreolus Saccharothrix mutabilis subsp. capreolus] and [https://en.wikipedia.org/wiki/Streptosporangium_roseum Streptosporangium roseum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8I82 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8I82 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]] 1.95&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=DPP:DIAMINOPROPANOIC+ACID'>DPP</scene>, <scene name='pdbligand=KBE:BETA-LYSINE'>KBE</scene>, <scene name='pdbligand=MYN:(2S)-AMINO[(4R)-2-AMINO-1,4,5,6-TETRAHYDROPYRIMIDIN-4-YL]ETHANOIC+ACID'>MYN</scene>, <scene name='pdbligand=UAL:(2Z)-2-AMINO-3-(CARBAMOYLAMINO)PROP-2-ENOIC+ACID'>UAL</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=8i82 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8i82 OCA], [https://pdbe.org/8i82 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8i82 RCSB], [https://www.ebi.ac.uk/pdbsum/8i82 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8i82 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/D2B3F1_STRRD D2B3F1_STRRD] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Metagenomic-based studies have predicted an extraordinary number of potential antibiotic-resistance genes (ARGs). These ARGs are hidden in various environmental bacteria and may become a latent crisis for antibiotic therapy via horizontal gene transfer. In this study, we focus on a resistance gene cph, which encodes a phosphotransferase (Cph) that confers resistance to the antituberculosis drug capreomycin (CMN). Sequence Similarity Network (SSN) analysis classified 353 Cph homologues into five major clusters, where the proteins in cluster I were found in a broad range of actinobacteria. We examine the function and antibiotics targeted by three putative resistance proteins in cluster I via biochemical and protein structural analysis. Our findings reveal that these three proteins in cluster I confer resistance to CMN, highlighting an important aspect of CMN resistance within this gene family. This study contributes towards understanding the sequence-structure-function relationships of the phosphorylation resistance genes that confer resistance to CMN.

Discovery and characterization of genes conferring natural resistance to the antituberculosis antibiotic capreomycin.,Toh SI, Elaine Keisha J, Wang YL, Pan YC, Jhu YH, Hsiao PY, Liao WT, Chen PY, Ko TM, Chang CY Commun Biol. 2023 Dec 19;6(1):1282. doi: 10.1038/s42003-023-05681-6. PMID:38114770<ref>PMID:38114770</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8i82" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharothrix mutabilis subsp. capreolus]]
[[Category: Streptosporangium roseum]]
[[Category: Chang CY]]
[[Category: Elaine K J]]
[[Category: Toh SI]]