PDBsum entry 5t7c

Membrane protein

PDB id: 5t7c

Contents

Protein chain

186 a.a.

PDB id:

5t7c

Name:

Membrane protein

Title:

Solution structure of calcium free, myristoylated visinin-like protein 3

Structure:

Hippocalcin-like protein 1. Chain: a. Synonym: calcium-binding protein bdr-1,hlp2,visinin-like protein 3, vilip-3. Engineered: yes. Other_details: myristoyl group is covalently attached to the n- terminal

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: hpcal1, bdr1. Expressed in: escherichia coli. Expression_system_taxid: 562

NMR struc:

10 models

Authors:

S.Lim,J.B.Ames

Key ref:

C.Li et al. (2016). Structure and Calcium Binding Properties of a Neuronal Calcium-Myristoyl Switch Protein, Visinin-Like Protein 3. PLoS One, 11, e0165921. PubMed id: 27820860 DOI: 10.1371/journal.pone.0165921

Date:

02-Sep-16 Release date: 12-Jul-17

Protein chain

P37235  (HPCL1_HUMAN) -  Hippocalcin-like protein 1 from Homo sapiens

Seq: 193 a.a.

Struc: 186 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

DOI no: 10.1371/journal.pone.0165921

PLoS One 11:e0165921 (2016)

PubMed id: 27820860

Structure and Calcium Binding Properties of a Neuronal Calcium-Myristoyl Switch Protein, Visinin-Like Protein 3.

C.Li, S.Lim, K.H.Braunewell, J.B.Ames.

ABSTRACT

Visinin-like protein 3 (VILIP-3) belongs to a family of Ca2+-myristoyl switch proteins that regulate signal transduction in the brain and retina. Here we analyze Ca2+ binding, characterize Ca2+-induced conformational changes, and determine the NMR structure of myristoylated VILIP-3. Three Ca2+ bind cooperatively to VILIP-3 at EF2, EF3 and EF4 (KD = 0.52 μM and Hill slope of 1.8). NMR assignments, mutagenesis and structural analysis indicate that the covalently attached myristoyl group is solvent exposed in Ca2+-bound VILIP-3, whereas Ca2+-free VILIP-3 contains a sequestered myristoyl group that interacts with protein residues (E26, Y64, V68), which are distinct from myristate contacts seen in other Ca2+-myristoyl switch proteins. The myristoyl group in VILIP-3 forms an unusual L-shaped structure that places the C14 methyl group inside a shallow protein groove, in contrast to the much deeper myristoyl binding pockets observed for recoverin, NCS-1 and GCAP1. Thus, the myristoylated VILIP-3 protein structure determined in this study is quite different from those of other known myristoyl switch proteins (recoverin, NCS-1, and GCAP1). We propose that myristoylation serves to fine tune the three-dimensional structures of neuronal calcium sensor proteins as a means of generating functional diversity.