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<i>Mtb</i>GlyRS and <i>Mtr</i>GlyRS purify predominantly as monomers.

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posted on 2025-06-30, 19:00 authored by Michael K. Fenwick, Amy E. DeRocher, Justin K. Craig, Elizabeth K. Harmon, Steve Seibold, Lijun Liu, Kevin P. Battaile, Lynn K. Barrett, Wesley C. Van Voorhis, Isabelle Q. Phan, Bart L. Staker, Sandhya Subramanian, Scott Lovell, Peter J. Myler
<p><b>(A)</b><i>Mtb</i>GlyRS purified using a HiLoad 26/600 Superdex 75 column runs mostly at 47.3 kDa. <b>(B)</b> <i>Mtr</i>GlyRS purified using a HiLoad 26/600 Superdex 200 column elutes with an apparent mass of 36.9 kDa.</p>

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    various liganded statesstructurally characterized previouslystructural genomics pipelinesize exclusion chromatographyseveral liganded statesprospective drug targetsdiv >< pbased drug discoverymycobacterium tuberculosis </mycobacterium thermoresitibile </mycobacterium thermoresistibile </mycobacterium smegmatis </escherichia coli </dimeric state characteristicglyrs apoenzyme crystalglycyl trna synthetasesmtr </mtb </trna synthetasesapo statetwo enzymessignificant portionsrecent worklid motifinsertion domainhuman glyrshuman enzymeglyrs ),dual targeteddimer interfacedespite crystallizingcrystal structuresadenosine monophosphate95 å85 å

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