PDB ID or protein name

1r3j » Potassium channel KcsA

1r3j » Potassium channel KcsA
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Topology in Bacterial Gram-positive plasma membrane
Topologyout side
in side
1r3j » Potassium channel KcsA
Hydrophobic Thickness 34.8 ± 1.2 Å
Tilt Angle 0 ± 0°
ΔGtransfer -111.0 kcal/mol
Links to 1r3j PDB Sum, PDB, SCOP, MSD, OCA, MMDB
Topology subunit C (N-terminus in)
Resolution 1.90 Å
Other PDB entries representing this structure 1bl8, 1f6g, 1j95, 1jq1, 1jvm, 1k4c, 1k4d, 1r3i, 1r3k, 1r3l, 1zwi, 2atk, 2bob, 2boc, 2dwd, 2dwe, 2h8p, 2hg5, 2hjf, 2hvj, 2hvk, 2ih1, 2ih3, 2itc, 2itd, 2jk5, 2nlj, 2p7t, 2qto, 2w0f, 3gb7, 3hpl, 3ifx, 3iga, 3ogc, 3or6, 3or7, 3stl, 3stz, 4lbe, 4lcu, 4msw
Number of TM Secondary Structures 8
4 transmembrane subunits
C - Tilt: 28° - Segments: 1(25-50), 2(86-111)
D - Tilt: 28° - Segments: 1(25-50), 2(86-111)
J - Tilt: 28° - Segments: 1(25-50), 2(86-111)
H - Tilt: 28° - Segments: 1(25-50), 2(86-111)
Experimental Verification for 1r3j » Potassium channel KcsA
Locations of hydrophobic boundary planes are consistent with spin-labeling (Perozo et al. 1998, Cross et al. 1999, Cross and Hubbell 2002) and hydrophobic matching (Williamson et al. 2002, 2003) studies of KcsA. Average tilt of TM helices (31°) is consistent with ATR FTIR data (33°)(Le Coutre et al. 1998).
6 references
Gross A, and Hubbell WL (2002) Identification of protein side chains near the membrane-aqueous interface: A site-directed spin labeling study of KcsA. Biochemistry 41: 1123-1128. PubMed
Gross A, Columbus L, Hideg K, Altenbach C, and Hubbell WL (1999) Structure of the KcsA potassium channel from Streptomyces lividans: A site-directed spin labeling study of the second transmembrane segment. Biochemistry 38: 10324-10335. PubMed
Le Coutre J, Kaback HR, Patel CKN, Heginbotham L, and Miller C (1998) Fourier transform infrared spectroscopy reveals a rigid alpha-helical assembly for the tetrameric Streptomyces lividans K+ channel. Proc. Natl. Acad. Sci. USA 95: 6114-6117. PubMed
Perozo E, Cortes DM, and Cuello LG (1998) Three-dimensional architecture and gating mechanism of a K+ channel studied by EPR spectroscopy Nature Struct. Biol. 5 (6): 459-469. PubMed
Williamson IM, Alvis SJ, East JM, and Lee AG (2002) Interactions of phospholipids with the potassium channel KcsA. Biophys. J. 83: 2026-2038. PubMed
Williamson IM, Alvis SJ, East JM, and Lee AG (2003) The potassium channel KcsA and its interaction with the lipid bilayer. Cell Mol. Life Sci. 60: 1581-1590.2. PubMed
Comments on 1r3j » Potassium channel KcsA
2k1e and 2kb2 are models of a water-soluble analogue; 1jq1 and 1jq2 are NMR models of a shorter segment. Several structures of the channel, which were deposited to the PDB without proper biomatrix (1zwi, 2atk, 2jk5, 2w0f and 3hpl), are taken from the PDBTM database.