PDBsum entry 2dgj

Cell adhesion

PDB id: 2dgj

Contents

Protein chains

246 a.a. *

Ligands

SO4 ×2

ACY

GOL

Waters ×280

* Residue conservation analysis

PDB id:

2dgj

Name:

Cell adhesion

Title:

Crystal structure of ebha (756-1003 domain) from staphylococcus aureus

Structure:

Hypothetical protein ebha. Chain: a, b. Fragment: residues 2-249. Engineered: yes

Source:

Staphylococcus aureus. Organism_taxid: 1280. Strain: mu50. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.35Å R-factor: 0.241 R-free: 0.287

Authors:

Y.Tanaka,M.Yao,M.Kuroda,N.Watanabe,T.Ohta,I.Tanaka

Key ref:

Y.Tanaka et al. (2008). A helical string of alternately connected three-helix bundles for the cell wall-associated adhesion protein Ebh from Staphylococcus aureus. Structure, 16, 488-496. PubMed id: 18334223 DOI: 10.1016/j.str.2007.12.018

Date:

14-Mar-06 Release date: 20-Mar-07

Protein chains

Q931R6  (EBHA_STAAM) -  Extracellular matrix-binding protein EbhA from Staphylococcus aureus (strain Mu50 / ATCC 700699)

Seq: 6713 a.a.

Struc: 246 a.a.*

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

DOI no: 10.1016/j.str.2007.12.018

Structure 16:488-496 (2008)

PubMed id: 18334223

A helical string of alternately connected three-helix bundles for the cell wall-associated adhesion protein Ebh from Staphylococcus aureus.

Y.Tanaka, S.Sakamoto, M.Kuroda, S.Goda, Y.G.Gao, K.Tsumoto, Y.Hiragi, M.Yao, N.Watanabe, T.Ohta, I.Tanaka.

ABSTRACT

The 1.1 MDa cell-wall-associated adhesion protein of staphylococci, Ebh, consists of several distinct regions, including a large central region with 52 imperfect repeats of 126 amino acid residues. We investigated the structure of this giant molecule by X-ray crystallography, circular dichroism (CD) spectrometry, and small-angle X-ray scattering (SAXS). The crystal structure of two repeats showed that each repeat consists of two distinct three-helix bundles, and two such repeats are connected along the long axis, resulting in a rod-like structure that is 120 A in length. CD and SAXS analyses of the samples with longer repeats suggested that each repeat has an identical structure, and that such repeats are connected tandemly to form a rod-like structure in solution, the length of which increased proportionately with the number of repeating units. On the basis of these results, it was proposed that Ebh is a 320 nm rod-like molecule with some plasticity at module junctions.

Selected figure(s)

Figure 1.
Figure 1. Crystal Structure of EbhA-R7-R8
(A) Ribbon diagram of EbhA-R7-R8. The ribbon model is colored according to the sequence, from blue at the N terminus to red at the C terminus. The repeating units are indicated.
(B) Topological diagram of EbhA-R7-R8. Squares indicate α helices. Colors correspond to those in (A).

Figure 6.
Figure 6. Low-Resolution Structures of EbhA-R7, EbhA-R7-R8, and EbhA-R5-R8
(A–C) Calculated low-resolution structures are shown as green balls. Crystal structures of (A) EbhA-R7 and (B) EbhA-R7-R8 superposed on those of low-resolution structures are also shown as red ribbon diagrams. The structure of (C) EbhA-R5-R8 inferred from the crystal structure of EbhA-R7-R8 is also shown as a red ribbon diagram. The lengths of low-resolution structures and structures deduced from the crystal structure of EbhA-R7-R8 are also indicated as green and red letters, respectively.

The above figures are reprinted by permission from Cell Press: Structure (2008, 16, 488-496) copyright 2008.

Figures were selected by an automated process.