1998
DOI: 10.1006/jmbi.1997.1544
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Crystal structure of the IIB subunit of a fructose permease (IIBLev) from Bacillus subtilis

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Cited by 40 publications
(44 citation statements)
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“…Sequential and side-chain assignments of IIA Mtl (H554Q) and phospho-IIB Mtl (C384S) in a 1:1 mixture were performed using three-dimensional triple resonance through-bond scalar correlation experiments (three-dimensional HNCACB, CBCA(CO)NH, HBHA(CBCACO)NH, C(CCO)NH, and H(CCO)NH) in conjunction with three-dimensional Side-chain torsion angle restraints were derived from 3 J NC␥ and 3 J CЈC␥ coupling constants measured using quantitative J correlation spectroscopy (27) in conjunction with short mixing time (30 ms) three-dimensional 13 C-separated NOE spectra recorded in H 2 O (26). Axially stretched (28) neutral polyacrylamide gels (5% (w/v) polyacrylamide; 39:1 (w/w) acrylamide/bisacrylamide) were prepared as described previously (21).…”
Section: Mtlmentioning
confidence: 99%
See 1 more Smart Citation
“…Sequential and side-chain assignments of IIA Mtl (H554Q) and phospho-IIB Mtl (C384S) in a 1:1 mixture were performed using three-dimensional triple resonance through-bond scalar correlation experiments (three-dimensional HNCACB, CBCA(CO)NH, HBHA(CBCACO)NH, C(CCO)NH, and H(CCO)NH) in conjunction with three-dimensional Side-chain torsion angle restraints were derived from 3 J NC␥ and 3 J CЈC␥ coupling constants measured using quantitative J correlation spectroscopy (27) in conjunction with short mixing time (30 ms) three-dimensional 13 C-separated NOE spectra recorded in H 2 O (26). Axially stretched (28) neutral polyacrylamide gels (5% (w/v) polyacrylamide; 39:1 (w/w) acrylamide/bisacrylamide) were prepared as described previously (21).…”
Section: Mtlmentioning
confidence: 99%
“…The coordinates of the backbone and noninterfacial side chains were held fixed, and rigid body docking with full torsional degrees of freedom for the interfacial side chains was driven by interproton distance restraints derived from intermolecular NOE data coupled with torsion angle restraints derived from both heteronuclear coupling constant and short mixing time NOE data. Examples of the quality of the intermolecular NOE data obtained from three-dimensional 13 C-separated/ 12 C-filtered NOE experiments that provide exclusively intermolecular NOEs from protons attached to 13 C on the 13 Clabeled protein to protons attached to 12 C on the unlabeled protein, are shown in Fig. 2.…”
Section: Number Of Experimental Nmr Restraintsmentioning
confidence: 99%
“…Crystal and NMR structures of the N-terminal domain of enzyme I (EIN) (5,6) and HPr (7-11) have been determined. Crystal and/or NMR structures from a variety of species have been solved for representatives of the IIA domains from all four classes (12)(13)(14)(15)(16) and the IIB domains from three of the four classes (17)(18)(19)(20)(21)(22), the exception being IIB Mtl . In addition, four cytoplasmic protein-protein complexes of the PTS have been solved by NMR: EIN-HPr (23), IIA Glc -HPr (24), IIA Glc -IIB Glc (22), and IIA Mtl -HPr (25).…”
mentioning
confidence: 99%
“…Protein Expression-The recombinant plasmids, pSP100 for HPr expression (20) and pLP1572 for IIA Mtl expression, were introduced into E. coli GI698 for protein expression induced by tryptophan (21). Four-liter cultures were grown in minimal labeling medium (MLM) (22) Protein Purification-E. coli HPr, unlabeled and/or isotopically labeled with 15 N (Ͼ95%) and 13 C (Ͼ95%), was purified as described elsewhere (17,23).…”
mentioning
confidence: 99%