4DHE

Crystal structure of a probable GTP-binding protein engB from Burkholderia thailandensis

Summary for 4DHE

• Entry DOI: 10.2210/pdb4dhe/pdb
• Descriptor: Probable GTP-binding protein EngB, CHLORIDE ION (3 entities in total)
• Functional Keywords: melioidosis, ras-like gtpase, cell division, cell cycle, septation, gtp-binding, structural genomics, seattle structural genomics center for infectious disease, ssgcid
• Biological source: Burkholderia thailandensis
• Total number of polymer chains: 2
• Total formula weight: 49182.52

Authors

Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2012-01-27, release date: 2012-02-08, 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 (2.2 Å)