Medizinische Universität Graz Austria/Österreich - Forschungsportal - Medical University of Graz
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SHR Neuro Krebs Kardio Lipid Stoffw Microb
Sinnige, T; Houben, K; Pritisanac, I; Renault, M; Boelens, R; Baldus, M.
Insight into the conformational stability of membrane-embedded BamA using a combined solution and solid-state NMR approach.
J Biomol NMR. 2015; 61(3-4):321-32
Doi: 10.1007/s10858-014-9891-6
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PubMed
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- Co-Autor*innen der Med Uni Graz
- Pritisanac Iva
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- Abstract:
- The β-barrel assembly machinery (BAM) is involved in folding and insertion of outer membrane proteins in Gram-negative bacteria, a process that is still poorly understood. With its 790 residues, BamA presents a challenge to current NMR methods. We utilized a "divide and conquer" approach in which we first obtained resonance assignments for BamA's periplasmic POTRA domains 4 and 5 by solution NMR. Comparison of these assignments to solid-state NMR (ssNMR) data obtained on two BamA constructs including the transmembrane domain and one or two soluble POTRA domains suggested that the fold of POTRA domain 5 critically depends on the interface with POTRA 4. Using specific labeling schemes we furthermore obtained ssNMR resonance assignments for residues in the extracellular loop 6 that is known to be crucial for BamA-mediated substrate folding and insertion. Taken together, our data provide novel insights into the conformational stability of membrane-embedded, non-crystalline BamA.
- Find related publications in this database (using NLM MeSH Indexing)
- Amino Acid Sequence - administration & dosage
- Bacterial Outer Membrane Proteins - chemistry, genetics, ultrastructure
- Escherichia coli - genetics, metabolism
- Escherichia coli Proteins - chemistry, genetics, ultrastructure
- Models, Molecular - administration & dosage
- Molecular Sequence Data - administration & dosage
- Nuclear Magnetic Resonance, Biomolecular - methods
- Protein Folding - administration & dosage
- Protein Structure, Tertiary - genetics
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- Find related publications in this database (Keywords)
- NMR spectroscopy
- Membrane proteins
- Proteoliposomes
- beta-Barrel assembly
- Protein dynamics