5HSP

MamM CTD M250L

Summary for 5HSP

• Entry DOI: 10.2210/pdb5hsp/pdb
• Descriptor: Magnetosome protein MamM, SULFATE ION (3 entities in total)
• Functional Keywords: cation diffusion facilitator, metal transport
• Biological source: Magnetospirillum gryphiswaldense
• Total number of polymer chains: 2
• Total formula weight: 27755.02

Authors

Barber-Zucker, S.,Zarivach, R. (deposition date: 2016-01-26, release date: 2016-11-30, Last modification date: 2024-01-10)

Primary citation

Barber-Zucker, S.,Uebe, R.,Davidov, G.,Navon, Y.,Sherf, D.,Chill, J.H.,Kass, I.,Bitton, R.,Schuler, D.,Zarivach, R.
Disease-Homologous Mutation in the Cation Diffusion Facilitator Protein MamM Causes Single-Domain Structural Loss and Signifies Its Importance.
Sci Rep, 6:31933-31933, 2016

PubMed Abstract: Cation diffusion facilitators (CDF) are highly conserved, metal ion efflux transporters that maintain divalent transition metal cation homeostasis. Most CDF proteins contain two domains, the cation transporting transmembrane domain and the regulatory cytoplasmic C-terminal domain (CTD). MamM is a magnetosome-associated CDF protein essential for the biomineralization of magnetic iron-oxide particles in magnetotactic bacteria. To investigate the structure-function relationship of CDF cytoplasmic domains, we characterized a MamM M250P mutation that is synonymous with the disease-related mutation L349P of the human CDF protein ZnT-10. Our results show that the M250P exchange in MamM causes severe structural changes in its CTD resulting in abnormal reduced function. Our in vivo, in vitro and in silico studies indicate that the CTD fold is critical for CDF proteins' proper function and support the previously suggested role of the CDF cytoplasmic domain as a CDF regulatory element. Based on our results, we also suggest a mechanism for the effects of the ZnT-10 L349P mutation in human.

PubMed: 27550551
DOI: 10.1038/srep31933

Experimental method

X-RAY DIFFRACTION (1.79 Å)