3LBS

Crystal structure of the cytoplasmic tail of (pro)renin receptor as a MBP fusion (Maltose-bound form)

Summary for 3LBS

• Entry DOI: 10.2210/pdb3lbs/pdb
• Related: 3LC8
• Related PRD ID: PRD_900001
• Descriptor: Maltose-binding periplasmic protein, Renin receptor, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose (3 entities in total)
• Functional Keywords: renin receptor, prorenin receptor, atp6ap2, cytoplasmic tail, maltose binding protein fusion, sugar transport, transport, transport protein
• Biological source: Escherichia coli; More
• Total number of polymer chains: 2
• Total formula weight: 85508.34

Authors

Zhang, Y.,Garavito, R.M. (deposition date: 2010-01-08, release date: 2011-02-16, Last modification date: 2023-09-06)

Primary citation

Zhang, Y.,Gao, X.,Michael Garavito, R.
Structural analysis of the intracellular domain of (pro)renin receptor fused to maltose-binding protein.
Biochem.Biophys.Res.Commun., 407:674-679, 2011

PubMed Abstract: The (pro)renin receptor (PRR) is an important component of the renin-angiotensin system (RAS), which regulates blood pressure and cardiovascular function. The integral membrane protein PRR contains a large extracellular domain (∼310 amino acids), a single transmembrane domain (∼20 amino acids) and an intracellular domain (∼19 amino acids). Although short, the intracellular (IC) domain of the PRR has functionally important roles in a number of signal transduction pathways activated by (pro)renin binding. Meanwhile, together with the transmembrane domain and a small portion of the extracellular domain (∼30 amino acids), the IC domain is also involved in assembly of V(0) portion of the vacuolar proton-translocating ATPase (V-ATPase). To better understand structural and multifunctional roles of the PRR-IC, we report the crystal structure of the PRR-IC domain as maltose-binding protein (MBP) fusion proteins at 2.0Å (maltose-free) and 2.15Å (maltose-bound). In the two separate crystal forms having significantly different unit-cell dimensions and molecular packing, MBP-PRR-IC fusion protein was found to be a dimer, which is different with the natural monomer of native MBP. The PRR-IC domain appears as a relatively flexible loop and is responsible for the dimerization of MBP fusion protein. Residues in the PRR-IC domain, particularly two tyrosines, dominate the intermonomer interactions, suggesting a role for the PRR-IC domain in protein oligomerization.

PubMed: 21420935
DOI: 10.1016/j.bbrc.2011.03.074

Experimental method

X-RAY DIFFRACTION (2.15 Å)