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4H3Y

Crystal structure of an asymmetric dimer of a tRNA (guanine-(N(1)-)-methyltransferase from Burkholderia phymatum bound to S-adenosyl homocystein in one half-site

Summary for 4H3Y
Entry DOI10.2210/pdb4h3y/pdb
Related4H3Z
DescriptortRNA (guanine-N(1)-)-methyltransferase, S-ADENOSYL-L-HOMOCYSTEINE, CHLORIDE ION, ... (4 entities in total)
Functional Keywordsstructural genomics, niaid, national institute of allergy and infectious diseases, seattle structural genomics center for infectious disease, ssgcid, trmd, m1g-methyltransferase, g37 methyltransferase, s-adenosyl-methionine, sam, s-adenosyl-homocysteine, sah, trna modification, transferase, proteobacteria, nitrogen fixation, food pathogen, domain swapped homodimer
Biological sourceBurkholderia phymatum
Cellular locationCytoplasm (Potential): B2JF31
Total number of polymer chains2
Total formula weight61997.72
Authors
Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2012-09-14, release date: 2012-10-03, Last modification date: 2023-09-20)
Primary citationBaugh, L.,Gallagher, L.A.,Patrapuvich, R.,Clifton, M.C.,Gardberg, A.S.,Edwards, T.E.,Armour, B.,Begley, D.W.,Dieterich, S.H.,Dranow, D.M.,Abendroth, J.,Fairman, J.W.,Fox, D.,Staker, B.L.,Phan, I.,Gillespie, A.,Choi, R.,Nakazawa-Hewitt, S.,Nguyen, M.T.,Napuli, A.,Barrett, L.,Buchko, G.W.,Stacy, R.,Myler, P.J.,Stewart, L.J.,Manoil, C.,Van Voorhis, W.C.
Combining functional and structural genomics to sample the essential Burkholderia structome.
Plos One, 8:e53851-e53851, 2013
Cited by
PubMed Abstract: The genus Burkholderia includes pathogenic gram-negative bacteria that cause melioidosis, glanders, and pulmonary infections of patients with cancer and cystic fibrosis. Drug resistance has made development of new antimicrobials critical. Many approaches to discovering new antimicrobials, such as structure-based drug design and whole cell phenotypic screens followed by lead refinement, require high-resolution structures of proteins essential to the parasite.
PubMed: 23382856
DOI: 10.1371/journal.pone.0053851
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

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数据于2025-07-02公开中

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