8F1B

Structure of zinc-bound ZrgA deletion 124-184 from Vibrio cholerae

Summary for 8F1B

• Entry DOI: 10.2210/pdb8f1b/pdb
• Related: 8EZW
• Descriptor: Zinc-binding protein, ZINC ION, TRIETHYLENE GLYCOL, ... (4 entities in total)
• Functional Keywords: zinc, abc transporter, solute binding protein, metal binding protein
• Biological source: Vibrio cholerae O1 biovar El Tor str. N16961; More
• Total number of polymer chains: 6
• Total formula weight: 110886.64

Authors

Valencia, D.W.,Yukl, E.T. (deposition date: 2022-11-04, release date: 2023-01-18, Last modification date: 2024-10-16)

Primary citation

Valencia, D.W.,Melendez, A.B.,Melendrez, I.A.,Yukl, E.T.
Structure and Function of the Zinc Binding Protein ZrgA from Vibrio cholerae.
Int J Mol Sci, 24:-, 2022

PubMed Abstract: ATP binding cassette (ABC) transporters are the primary means by which bacteria acquire trace elements from the environment. They rely on solute binding proteins (SBPs) to bind the relevant substrate and deliver it to the integral membrane permease for ATP-powered import into the cytoplasm. SBPs of cluster A-I are known to facilitate the transport of essential metals zinc, manganese, and iron, and many have been characterized to date. A group of ABC transporter operons dubbed zinc-regulated genes () have recently been shown to transport zinc with putative SBPs () bearing no homology to the classical cluster A-I family, and a recent crystal structure of a representative protein from shows no structural similarity to classical SBPs. Thus, the ZrgA proteins appear to represent a newly discovered family of zinc SBPs widespread among Gram-negative bacteria, including human pathogens. Here, we have determined the crystal structure of ZrgA from and characterized its zinc binding in vitro and function in vivo. We also assessed the role of a histidine-rich sequence that appears to be a hallmark of ZrgA proteins that is particularly long in ZrgA. The results show that the gene is critical to the function of the operon, consistent with a function as an SBP in this system. Further, the His-rich region is not essential to the function of ZrgA, but it does provide additional zinc binding sites in vitro. The structure and zinc binding data for ZrgA reveal interesting differences between it and its homologue from , illustrating diversity within this little-studied protein family.

PubMed: 36613986
DOI: 10.3390/ijms24010548

Experimental method

X-RAY DIFFRACTION (2.41 Å)