PDBsum entry 1avr

Calcium/phospholipid binding

PDB id: 1avr

Contents

Protein chain

317 a.a. *

Ligands

SO4 ×2

Metals

_CA ×5

Waters ×202

* Residue conservation analysis

PDB id:

1avr

Name:

Calcium/phospholipid binding

Title:

Crystal and molecular structure of human annexin v after refinement. Implications for structure, membrane binding and ion channel formation of the annexin family of proteins

Structure:

Annexin v. Chain: a. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606

Resolution:

2.30Å R-factor: 0.184

Authors:

R.Huber,R.Berendes,A.Burger,M.Schneider,A.Karshikov,H.Luecke, J.Roemisch,E.Paques

Key ref:

R.Huber et al. (1992). Crystal and molecular structure of human annexin V after refinement. Implications for structure, membrane binding and ion channel formation of the annexin family of proteins. J Mol Biol, 223, 683-704. PubMed id: 1311770 DOI: 10.1016/0022-2836(92)90984-R

Date:

17-Oct-91 Release date: 31-Jan-94

Protein chain

P08758  (ANXA5_HUMAN) -  Annexin A5 from Homo sapiens

Seq: 320 a.a.

Struc: 317 a.a.

DOI no: 10.1016/0022-2836(92)90984-R

J Mol Biol 223:683-704 (1992)

PubMed id: 1311770

Crystal and molecular structure of human annexin V after refinement. Implications for structure, membrane binding and ion channel formation of the annexin family of proteins.

R.Huber, R.Berendes, A.Burger, M.Schneider, A.Karshikov, H.Luecke, J.Römisch, E.Paques.

ABSTRACT

Two crystal forms (P6(3) and R3) of human annexin V have been crystallographically refined at 2.3 A and 2.0 A resolution to R-values of 0.184 and 0.174, respectively, applying very tight stereochemical restraints with deviations from ideal geometry of 0.01 A and 2 degrees. The three independent molecules (2 in P6(3), 1 in R3) are similar, with deviations in C alpha positions of 0.6 A. The polypeptide chain of 320 amino acid residues is folded into a planar cyclic arrangement of four repeats. The repeats have similar structures of five alpha-helical segments wound into a right-handed compact superhelix. Three calcium ion sites in repeats I, II and IV and two lanthanum ion sites in repeat I have been found in the R3 crystals. They are located at the convex face of the molecule opposite the N terminus. Repeat III has a different conformation at this site and no calcium bound. The calcium sites are similar to the phospholipase A2 calcium-binding site, suggesting analogy also in phospholipid interaction. The center of the molecule is formed by a channel of polar charged residues, which also harbors a chain of ordered water molecules conserved in the different crystal forms. Comparison with amino acid sequences of other annexins shows a high degree of similarity between them. Long insertions are found only at the N termini. Most conserved are the residues forming the metal-binding sites and the polar channel. Annexins V and VII form voltage-gated calcium ion channels when bound to membranes in vitro. We suggest that annexins bind with their convex face to membranes, causing local disorder and permeability of the phospholipid bilayers. Annexins are Janus-faced proteins that face phospholipid and water and mediate calcium transport.

Selected figure(s)

Figure 4.
Figure 4. uperposition of he alcium inding site f phospholipase A, with site Cal of nnexin V. ----. phospholipase A,; e, annexin.

Figure 7.
IIE

The above figures are reprinted by permission from Elsevier: J Mol Biol (1992, 223, 683-704) copyright 1992.

Figures were selected by an automated process.