View source for 8vxb


==Structure of ANT(6)-Ib from Campylobacter fetus subsp fetus complexed with hydrated streptomycin==
<StructureSection load='8vxb' size='340' side='right'caption='[[8vxb]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8vxb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Campylobacter_fetus_subsp._fetus Campylobacter fetus subsp. fetus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8VXB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8VXB 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]] 1.85&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5I0:[(2~{S},3~{S},4~{S},5~{R},6~{S})-2-[(2~{R},3~{R},4~{R},5~{S})-2-[(1~{R},2~{S},3~{R},4~{R},5~{S},6~{R})-2,4-bis[[azaniumylidene(azanyl)methyl]amino]-3,5,6-tris(oxidanyl)cyclohexyl]oxy-4-[bis(oxidanyl)methyl]-5-methyl-4-oxidanyl-oxolan-3-yl]oxy-6-(hydroxymethyl)-4,5-bis(oxidanyl)oxan-3-yl]-methyl-azanium'>5I0</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=8vxb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8vxb OCA], [https://pdbe.org/8vxb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8vxb RCSB], [https://www.ebi.ac.uk/pdbsum/8vxb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8vxb ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/D8L9Z0_CAMFE D8L9Z0_CAMFE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Aminoglycoside antibiotics have played a critical role in the treatment of both Gram-negative and Gram-positive bacterial infections. However, antibiotic resistance has severely compromised the efficacy of aminoglycosides. A leading cause of aminoglycoside resistance is mediated by bacterial enzymes that inactivate these drugs via chemical modification. Aminoglycoside nucleotidyltransferase-6 (ANT(6)) enzymes inactivate streptomycin by transferring an adenyl group from ATP to position 6 on the antibiotic. Despite the clinical significance of this activity, ANT(6) enzymes remain relatively uncharacterized. Here, we report the first high resolution x-ray crystallographic structure of ANT(6)-Ib from Campylobacter fetus subsp. fetus bound with streptomycin. Structural modeling and gel filtration chromatography experiments suggest that the enzyme exists as a dimer in which both subunits contribute to the active site. Moreover, superposition of the ANT(6)-Ib structure with the structurally related enzyme lincosamide nucleotidyltransferase B (LinB) permitted the identification of a putative nucleotide binding site. These data also suggest that residues D44 and D46 coordinate essential divalent metal ions and D102 functions as the catalytic base.

Structural and Biochemical Characterization of Aminoglycoside Nucleotidyltransferase(6)-Ib From Campylobacter fetus subsp. fetus.,Nalam P, Cook PD, Smith BA Proteins. 2024 Sep 9. doi: 10.1002/prot.26745. PMID:39246239<ref>PMID:39246239</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8vxb" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Campylobacter fetus subsp. fetus]]
[[Category: Large Structures]]
[[Category: Cook P]]
[[Category: Nalam P]]
[[Category: Smith B]]