PDBsum entry 1z47

Ligand binding protein

PDB id: 1z47

Contents

Protein chains

345 a.a. *

Metals

_CL ×2

Waters ×326

* Residue conservation analysis

PDB id:

1z47

Name:

Ligand binding protein

Title:

Structure of the atpase subunit cysa of the putative sulfate atp- binding cassette (abc) transporter from alicyclobacillus acidocaldarius

Structure:

Putative abc-transporter atp-binding protein. Chain: a, b. Synonym: cysa. Engineered: yes

Source:

Alicyclobacillus acidocaldarius. Organism_taxid: 405212. Gene: cysa. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.90Å R-factor: 0.225 R-free: 0.277

Authors:

F.Scheffel,U.Demmer,E.Warkentin,A.Huelsmann,E.Schneider,U.Ermler

Key ref:

F.Scheffel et al. (2005). Structure of the ATPase subunit CysA of the putative sulfate ATP-binding cassette (ABC) transporter from Alicyclobacillus acidocaldarius. FEBS Lett, 579, 2953-2958. PubMed id: 15893314 DOI: 10.1016/j.febslet.2005.04.017

Date:

15-Mar-05 Release date: 07-Jun-05

Protein chains

Q9RHZ7  (Q9RHZ7_ALIAC) -  Putative ABC-transporter ATP-binding protein from Alicyclobacillus acidocaldarius subsp. acidocaldarius

Seq: 343 a.a.

Struc: 345 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1016/j.febslet.2005.04.017

FEBS Lett 579:2953-2958 (2005)

PubMed id: 15893314

Structure of the ATPase subunit CysA of the putative sulfate ATP-binding cassette (ABC) transporter from Alicyclobacillus acidocaldarius.

F.Scheffel, U.Demmer, E.Warkentin, A.Hülsmann, E.Schneider, U.Ermler.

ABSTRACT

CysA, the ATPase subunit of a putative sulfate ATP-binding cassette transport system of the gram-positive thermoacidophilic bacterium Alicyclobacillus acidocaldarius, was structurally characterized at a resolution of 2.0 Angstroms in the absence of nucleotides. In line with previous findings on ABC-ATPases the structures of the two monomers (called CysA-1 and CysA-2) in the asymmetric unit differ substantially in the arrangement of their individual (sub)domains. CysA-2 was found as a physiological dimer composed of two crystallographically related monomers that are arranged in an open state. Interestingly, while the regulatory domain of CysA-2 packs against its opposing domain that of CysA-1 undergoes a conformational change and, in the dimer, would interfere with the opposing monomer thereby preventing solute translocation. Whether this conformational state is used for regulatory purposes will be discussed.

Selected figure(s)

Figure 1.
Fig. 1. Structure of CysA: (a) Ribbon diagram of the CysA monomer. The catalytic subdomain of the nucleotide-binding domain is shown in purple, the helical subdomain in red, the linker region in yellow and the regulatory domain in blue (distal β-sandwich) and royal blue (proximal β-sandwich). The location of conserved sequence motifs is indicated by capital letters: ‘Walker’ sites (A, B), D-loop, Q-loop, ABC signature (LSQ), and H motif. (b) Stereo representation of the CysA-2 dimer found in an open state. The monomers were shown in blue and red. For comparison CysA-2 was superimposed with the MalK[eco](open) structure at the front side (red) and with the MalK[eco](close) structure at the back side (green). In addition, the regulatory domains of the CysA-1 monomers are shown in yellow after superimposing with the catalytic domain. Fig. 1 and Fig. 2 have the same orientation and were generated using BOBSCRIPT [32].

Figure 2.
Fig. 2. Structural variability of the regulatory domains of CysA-1 (light-blue), CysA-2 (blue), MalK[tli] (yellow) and GlcV (pink). The regulatory domains undergo different conformational changes relative to the catalytic domain; however, the rotation axis and the direction of translation are conserved. The rotation axis passes perpendicular through helix L2 and the translation occurs parallel to the rotation axis.

The above figures are reprinted by permission from the Federation of European Biochemical Societies: FEBS Lett (2005, 579, 2953-2958) copyright 2005.

Figures were selected by an automated process.