4H3Z
Crystal structure of a symmetric dimer of a tRNA (guanine-(N(1)-)-methyltransferase from Burkholderia phymatum bound to S-adenosyl homocystein in both half-sites
Summary for 4H3Z
| Entry DOI | 10.2210/pdb4h3z/pdb |
| Related | 4H3Y |
| Descriptor | tRNA (guanine-N(1)-)-methyltransferase, S-ADENOSYL-L-HOMOCYSTEINE, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | structural genomics, niaid, national institute of allergy and infectious diseases, seattle structural genomics center for infectious disease, ssgcid, trna methylation, m1g37 methylation, transferase, sah, sam, food parasite |
| Biological source | Burkholderia phymatum |
| Cellular location | Cytoplasm (Potential): B2JF31 |
| Total number of polymer chains | 2 |
| Total formula weight | 62417.58 |
| 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 citation | Baugh, 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: 23382856DOI: 10.1371/journal.pone.0053851 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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