8ZTQ

Crystal structure of Sufu from Mycoplasma Pneumonia

Summary for 8ZTQ

• Entry DOI: 10.2210/pdb8ztq/pdb
• Related: 8ZTP
• Descriptor: Nitrogen fixation protein NifU, ZINC ION (3 entities in total)
• Functional Keywords: sufs, mycoplasma pneumonia, plp-binding, l-cys, biosynthetic protein
• Biological source: Mycoplasmoides pneumoniae 19294
• Total number of polymer chains: 2
• Total formula weight: 35929.40

Authors

Wang, W.M.,Ma, D.Y.,Gong, W.J.,Yao, H.,Liu, Y.H.,Wang, H.F. (deposition date: 2024-06-07, release date: 2024-12-11, Last modification date: 2024-12-18)

Primary citation

Ma, D.,Yao, H.,Liu, Y.,Gong, W.,Zhao, Y.,Wang, R.,Wu, C.,Wang, W.,Wang, H.
The reduced interaction between SufS and SufU in Mycoplasma penetrans results in diminished sulfotransferase activity.
Int.J.Biol.Macromol., 284:138181-138181, 2024

PubMed Abstract: Mycoplasma Penetrans (Mpe) is an AIDS-related mycoplasma that is also closely related to respiratory diseases. Proteins involved in the first phase of Fe-S cluster biosynthesis in the SUF-like pathway are essential in Gram-positive bacteria because there is no redundant Fe-S cluster biosynthetic pathway in these proteins. In this study, we characterized two essential proteins: cysteine desulphurase (MpeSufS) and sulfurtransferase (MpeSufU) in Mpe, and resolved their crystal structures. Our results reveal that MpeSufS belongs to type II cysteine desulfurase, and MpeSufU is a Zn-containing sulfurtransferase. Residue Q342 in MpeSufS and the zinc atom in MpeSufU mediate sulfur transfer from MpeSufS to MpeSufU. Mutation of Q342 significantly impacts the cysteine desulfurase activity. This study provides new insights into the regulation of the activity of the SufS-SufU complex, which will help guide the design of drugs for the treatment of mycoplasma infections.

PubMed: 39615726
DOI: 10.1016/j.ijbiomac.2024.138181

Experimental method

X-RAY DIFFRACTION (2.889 Å)