Subunit architecture.

(A) Amino acid residues modelled into electron density maps. Ranges of unstructured residues are listed above the sequences. (B) Structural domains and glycyl-AMS binding elements in MtbGlyRS. Catalytic domain, residues 1-87 and 144-3...

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التفاصيل البيبلوغرافية
المؤلف الرئيسي:	Michael K. Fenwick (1663099) (author)
مؤلفون آخرون:	Amy E. DeRocher (698177) (author), Justin K. Craig (10687219) (author), Elizabeth K. Harmon (21627186) (author), Steve Seibold (9428067) (author), Lijun Liu (452265) (author), Kevin P. Battaile (418240) (author), Lynn K. Barrett (293068) (author), Wesley C. Van Voorhis (10332534) (author), Isabelle Q. Phan (17132106) (author), Bart L. Staker (244387) (author), Sandhya Subramanian (348582) (author), Scott Lovell (122251) (author), Peter J. Myler (244412) (author)
منشور في:	2025
الموضوعات:	Biophysics Biochemistry Molecular Biology Pharmacology Infectious Diseases Biological Sciences not elsewhere classified Chemical Sciences not elsewhere classified various liganded states structurally characterized previously structural genomics pipeline size exclusion chromatography several liganded states prospective drug targets div >< p based drug discovery mycobacterium tuberculosis </ mycobacterium thermoresitibile </ mycobacterium thermoresistibile </ mycobacterium smegmatis </ escherichia coli </ dimeric state characteristic glyrs apoenzyme crystal glycyl trna synthetases mtr </ mtb </ trna synthetases apo state two enzymes significant portions recent work lid motif insertion domain human glyrs human enzyme glyrs ), dual targeted dimer interface despite crystallizing crystal structures adenosine monophosphate 95 å 85 å
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Subunit architecture.

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