PDBsum entry: 1m7k

Chaperone

PDB id: 1m7k

Contents

Protein chain

81 a.a. *

* Residue conservation analysis

PDB id:

1m7k

Name:

Chaperone

Title:

Solution structure of the sodd bag domain

Structure:

Silencer of death domains. Chain: a. Fragment: residues 358-456. Synonym: bag-family molecular chaperone regulator-4. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.

NMR struc:

20 models

Authors:

C.Brockmann,D.Leitner,D.Labudde,A.Diehl,V.Sievert,K.Buessow, H.Oschkinat

Key ref:

C.Brockmann et al. (2004). The solution structure of the SODD BAG domain reveals additional electrostatic interactions in the HSP70 complexes of SODD subfamily BAG domains. FEBS Lett, 558, 101-106. PubMed id: 14759524 DOI: 10.1016/S0014-5793(03)01490-X

Date:

22-Jul-02 Release date: 07-Aug-02

Protein chain

O95429  (BAG4_HUMAN) -  BAG family molecular chaperone regulator 4

Seq: 457 a.a.

Struc: 81 a.a.

 Gene Ontology (GO) functional annotation 

• Biochemical function: chaperone binding (1 term)

DOI no: 10.1016/S0014-5793(03)01490-X

FEBS Lett 558:101-106 (2004)

PubMed id: 14759524

The solution structure of the SODD BAG domain reveals additional electrostatic interactions in the HSP70 complexes of SODD subfamily BAG domains.

C.Brockmann, D.Leitner, D.Labudde, A.Diehl, V.Sievert, K.Büssow, R.Kühne, H.Oschkinat.

ABSTRACT

The solution structure of an N-terminally extended construct of the SODD BAG domain was determined by nuclear magnetic resonance spectroscopy. A homology model of the SODD-BAG/HSP70 complex reveals additional possible interactions that are specific for the SODD subfamily of BAG domains while the overall geometry of the complex remains the same. Relaxation rate measurements show that amino acids N358-S375 of SODD which were previously assigned to its BAG domain are not structured in our construct. The SODD BAG domain is thus indeed smaller than the homologous domain in Bag1 defining a new subfamily of BAG domains.

Selected figure(s)

Figure 4.
Fig. 4. Structural alignment. Structures of SODD and hBag1 (taken from 1HX1) BAG domains were aligned using the backbone atoms of residues 414, 420, 424, 435, 438, 446 and 453 in SODD and the corresponding residues in hBag1 which were shown to mediate the interaction with HSP70. The figure shows the binding interface (a) and the view from the N-terminus (b) rotated by 90° relative to a. Figure generated with MOLMOL.

Figure 5.
Fig. 5. Comparison of surface properties of the BAG domains of hBag1 and SODD. Surfaces of the BAG domains of hBag1 (a,b,d, taken from 1HX1) and SODD (c,e). In (a) the contact area of hBag1 to HSP70 in the crystal structure is depicted in orange. The conservation profile is mapped on the surface of the BAG domains in (b) and (c). Residues are colored as indicated in the text. In (d) and (e) the surfaces are colored according to electrostatic potential. The orientation is the same as in Fig. 3. Parts (b) and (c) were generated with MOLMOL.

The above figures are reprinted by permission from the Federation of European Biochemical Societies: FEBS Lett (2004, 558, 101-106) copyright 2004.

Figures were selected by an automated process.