| MWexperimental | 117 | kDa |
| MWexpected | 136 | kDa |
| VPorod | 123 | nm3 |
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log I(s)
3.27×10-2
3.27×10-3
3.27×10-4
3.27×10-5
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s, nm-1
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Structural basis for recruitment of peptidoglycan endopeptidase MepS by lipoprotein NlpI.
Wang S, Huang CH, Lin TS, Yeh YQ, Fan YS, Wang SW, Tseng HC, Huang SJ, Chang YY, Jeng US, Chang CI, Tzeng SR, Nat Commun 15(1):5461 (2024) Europe PMCSASDVW3 – Lipoprotein NlpI dimer bound to two asymmetrical murein DD-endopeptidase mMepS dimers at pH 7.0
Lipoprotein NlpIMurein DD-endopeptidase MepS/Murein LD-carboxypeptidase
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Fits and models
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Synchrotron SAXS data from solutions of NlpI dimer bound to two asymmetrical mMepS dimers in 0.2 M Na/K phosphate pH 7.0, 2 mM 2-mercaptoethanol, were collected on the TPS13A beam line at the NSRRC (Hsinchu, Taiwan) using a Eiger X 1M & 9M detector at a sample-detector distance of 2.5 m and at a wavelength of λ = 0.0826 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 100.00 μl sample at 10 mg/ml was injected at a 0.20 ml/min flow rate onto a Agilent Bio SEC-3, 300 Å column at 10°C. 210 successive 2 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.
Note: There is a discrepancy between the calculated molecular weight of the fully formed complex (136 kDa) compared to the experimentally determined molecular weight (117 kDa). |
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