7CDW

Crystal Structure of Mycobacterium Tuberculosis Elongation Factor G1

Summary for 7CDW

• Entry DOI: 10.2210/pdb7cdw/pdb
• Descriptor: Elongation factor G, GUANOSINE-5'-DIPHOSPHATE (2 entities in total)
• Functional Keywords: gtpase;elongation factor g(ef-g); ribosome-bound ef-g; crystal structure; antituberculosis drugs;, hydrolase
• Biological source: Mycobacterium tuberculosis H37Rv
• Total number of polymer chains: 2
• Total formula weight: 159507.61

Authors

Gao, X.,Cui, S. (deposition date: 2020-06-20, release date: 2021-09-22, Last modification date: 2022-02-16)

Primary citation

Gao, X.,Yu, X.,Zhu, K.,Qin, B.,Wang, W.,Han, P.,Aleksandra Wojdyla, J.,Wang, M.,Cui, S.
Crystal Structure of Mycobacterium tuberculosis Elongation Factor G1.
Front Mol Biosci, 8:667638-667638, 2021

PubMed Abstract: () caused an estimated 10 million cases of tuberculosis and 1.2 million deaths in 2019 globally. The increasing emergence of multidrug-resistant and extensively drug-resistant is becoming a public health threat worldwide and makes the identification of anti- drug targets urgent. Elongation factor G (EF-G) is involved in tRNA translocation on ribosomes during protein translation. Therefore, EF-G is a major focus of structural analysis and a valuable drug target of antibiotics. However, the crystal structure of EF-G1 is not yet available, and this has limited the design of inhibitors. Here, we report the crystal structure of Mtb EF-G1 in complex with GDP. The unique crystal form of the Mtb EF-G1-GDP complex provides an excellent platform for fragment-based screening using a crystallographic approach. Our findings provide a structure-based explanation for GDP recognition, and facilitate the identification of EF-G1 inhibitors with potential interest in the context of drug discovery.

PubMed: 34540889
DOI: 10.3389/fmolb.2021.667638

Experimental method

X-RAY DIFFRACTION (3 Å)