2KSD

Backbone structure of the membrane domain of E. coli histidine kinase receptor ArcB, Center for Structures of Membrane Proteins (CSMP) target 4310C

Summary for 2KSD

• Entry DOI: 10.2210/pdb2ksd/pdb
• NMR Information: BMRB: 16947
• Descriptor: Aerobic respiration control sensor protein arcB (1 entity in total)
• Functional Keywords: methods development, histidine kinase receptor, membrane domain, two-helical hairpin, cell-free synthesis, cell inner membrane, cell membrane, kinase, transcription, transcription regulation, transferase, transmembrane, two-component regulatory system, structural genomics, psi-2, protein structure initiative, center for structures of membrane proteins, csmp
• Biological source: Escherichia coli
• Cellular location: Cell inner membrane; Multi-pass membrane protein: P0AEC3
• Total number of polymer chains: 1
• Total formula weight: 13303.97

Authors

Maslennikov, I.,Klammt, C.,Hwang, E.,Kefala, G.,Kwiatkowski, W.,Jeon, Y.,Choe, S.,Center for Structures of Membrane Proteins (CSMP) (deposition date: 2010-01-02, release date: 2010-03-02, Last modification date: 2024-05-01)

Primary citation

Maslennikov, I.,Klammt, C.,Hwang, E.,Kefala, G.,Okamura, M.,Esquivies, L.,Mors, K.,Glaubitz, C.,Kwiatkowski, W.,Jeon, Y.H.,Choe, S.
Membrane domain structures of three classes of histidine kinase receptors by cell-free expression and rapid NMR analysis.
Proc.Natl.Acad.Sci.USA, 107:10902-10907, 2010

PubMed Abstract: NMR structural studies of membrane proteins (MP) are hampered by complications in MP expression, technical difficulties associated with the slow process of NMR spectral peak assignment, and limited distance information obtainable for transmembrane (TM) helices. To overcome the inherent challenges in the determination of MP structures, we have developed a rapid and cost-efficient strategy that combines cell-free (CF) protein synthesis, optimized combinatorial dual-isotope labeling for nearly instant resonance assignment, and fast acquisition of long-distance information using paramagnetic probes. Here we report three backbone structures for the TM domains of the three classes of Escherichia coli histidine kinase receptors (HKRs). The ArcB and QseC TM domains are both two-helical motifs, whereas the KdpD TM domain comprises a four-helical bundle with shorter second and third helices. The interhelical distances (up to 12 A) reveal weak interactions within the TM domains of all three receptors. Determined consecutively within 8 months, these structures offer insight into the abundant and underrepresented in the Protein Data Bank class of 2-4 TM crossers and demonstrate the efficiency of our CF combinatorial dual-labeling strategy, which can be applied to solve MP structures in high numbers and at a high speed. Our results greatly expand the current knowledge of HKR structure, opening the doors to studies on their widespread and pharmaceutically important bacterial signaling mechanism.

PubMed: 20498088
DOI: 10.1073/pnas.1001656107

Experimental method

SOLUTION NMR