PDB ID or protein name

1nqe » Outer membrane cobalamin transporter BtuB

1nqe » Outer membrane cobalamin transporter BtuB
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Topology in Bacterial Gram-negative outer membrane
Topologyout side
in side
1nqe » Outer membrane cobalamin transporter BtuB
Hydrophobic Thickness 23.4 ± 1.0 Å
Tilt Angle 5 ± 0°
ΔGtransfer -68.8 kcal/mol
Links to 1nqe PDB Sum, PDB, SCOP, MSD, OCA, MMDB
Topology subunit A (N-terminus in)
Resolution 2.00 Å
Other PDB entries of this protein 1nqf, 1nqg, 1nqh, 3m8b, 3m8d, 3rgm, 3rgn
Number of TM Secondary Structures 22
1 transmembrane subunit
A - Tilt: 1° - Segments: 1(136-145), 2(149-158), 3(164-173), 4(201-209), 5(214-222), 6(249-257), 7(261-269), 8(297-306), 9(309-316), 10(339-348), 11(351-359), 12(371-378), 13(383-390), 14(418-426), 15(429-436), 16(464-472), 17(475-482), 18(503-510), 19(514-521), 20(547-554), 21(559-566), 22(586-593)
Experimental Verification for 1nqe » Outer membrane cobalamin transporter BtuB
Locations of hydrophobic boundaries are consistent with site-directed spin-labeling studies (Fanucci et al. 2002).
1 reference
Fanucci GE, Cadieux N, Piedmont CA, Kadner RJ, and Cafiso DS (2002) Structure and dynamics of the beta-barrel of the membrane by site-directed spin labeling. Biochemistry 41: 11543-11551. PubMed
Comments on 1nqe » Outer membrane cobalamin transporter BtuB
Involved in the active translocation of vitamin B12 (cyanocobalamin) across the outer membrane to the periplasmic space. It derives its energy for transport by interacting with the trans-periplasmic membrane protein tonB. Is also a receptor for bacteriophages BF23 and C1, and for A and E colicins.