3HZU

Crystal structure of probable thiosulfate sulfurtransferase SSEA (rhodanese) from Mycobacterium tuberculosis

Summary for 3HZU

• Entry DOI: 10.2210/pdb3hzu/pdb
• Related: 3HWI
• Descriptor: Thiosulfate sulfurtransferase sseA, GLYCEROL, SULFATE ION, ... (4 entities in total)
• Functional Keywords: niaid, ssgcid, infectious disease, tuberculosis, transferase, structural genomics, seattle structural genomics center for infectious disease
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 1
• Total formula weight: 35838.04

Authors

Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2009-06-24, release date: 2009-07-07, Last modification date: 2023-09-06)

Primary citation

Edwards, T.E.,Liao, R.,Phan, I.,Myler, P.J.,Grundner, C.
Mycobacterium thermoresistibile as a source of thermostable orthologs of Mycobacterium tuberculosis proteins.
Protein Sci., 21:1093-1096, 2012

PubMed Abstract: The genus Mycobacterium comprises major human pathogens such as the causative agent of tuberculosis, Mycobacterium tuberculosis (Mtb), and many environmental species. Tuberculosis claims ~1.5 million lives every year, and drug resistant strains of Mtb are rapidly emerging. To aid the development of new tuberculosis drugs, major efforts are currently under way to determine crystal structures of Mtb drug targets and proteins involved in pathogenicity. However, a major obstacle to obtaining crystal structures is the generation of well-diffracting crystals. Proteins from thermophiles can have better crystallization and diffraction properties than proteins from mesophiles, but their sequences and structures are often divergent. Here, we establish a thermophilic mycobacterial model organism, Mycobacterium thermoresistibile (Mth), for the study of Mtb proteins. Mth tolerates higher temperatures than Mtb or other environmental mycobacteria such as M. smegmatis. Mth proteins are on average more soluble than Mtb proteins, and comparison of the crystal structures of two pairs of orthologous proteins reveals nearly identical folds, indicating that Mth structures provide good surrogates for Mtb structures. This study introduces a thermophile as a source of protein for the study of a closely related human pathogen and marks a new approach to solving challenging mycobacterial protein structures.

PubMed: 22544630
DOI: 10.1002/pro.2084

Experimental method

X-RAY DIFFRACTION (2.1 Å)