3V2I

Structure of a Peptidyl-tRNA hydrolase (PTH) from Burkholderia thailandensis

Summary for 3V2I

• Entry DOI: 10.2210/pdb3v2i/pdb
• Descriptor: Peptidyl-tRNA hydrolase, CITRIC ACID, UNKNOWN LIGAND, ... (4 entities in total)
• Functional Keywords: ssgcid, seattle structural genomics center for infectious disease, rna, peptidyl-trna hydrolase, hydrolase
• Biological source: Burkholderia thailandensis E264
• Cellular location: Cytoplasm (By similarity): Q2T1B9
• Total number of polymer chains: 1
• Total formula weight: 24617.04

Authors

Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2011-12-12, release date: 2012-01-11, Last modification date: 2023-09-13)

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

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

Experimental method

X-RAY DIFFRACTION (1.65 Å)