spacer
spacer

PDBsum entry 3c9l

Go to PDB code: 
Top Page protein ligands metals links
Signaling protein PDB id
3c9l
Contents
Protein chain
329 a.a.
Ligands
NAG-NAG-BMA ×2
ACE
RET
PLM ×2
PEF
LDA
C8E ×6
Metals
_ZN
Waters ×20

References listed in PDB file
Key reference
Title Alternative models for two crystal structures of bovine rhodopsin.
Author R.E.Stenkamp.
Ref. Acta Crystallogr D Biol Crystallogr, 2008, , 902-904.
PubMed id 18645239
Abstract
The space-group symmetry of two crystal forms of rhodopsin (PDB codes 1gzm and 2j4y; space group P3(1)) can be re-interpreted as hexagonal (space group P6(4)). Two molecules of the G protein-coupled receptor are present in the asymmetric unit in the trigonal models. However, the noncrystallographic twofold axes parallel to the c axis can be treated as crystallographic symmetry operations in the hexagonal space group. This halves the asymmetric unit and makes all of the protein molecules equivalent in these structures. Corrections for merohedral twinning were also applied in the refinement in the higher symmetry space group for one of the structures (2j4y).
Secondary reference #1
Title Structure of bovine rhodopsin in a trigonal crystal form.
Authors J.Li, P.C.Edwards, M.Burghammer, C.Villa, G.F.Schertler.
Ref. J Mol Biol, 2004, 343, 1409-1438. [DOI no: 10.1016/j.jmb.2004.08.090]
PubMed id 15491621
Full text Abstract
Figure 5.
Figure 5. A transmembrane slice showing H-bonding networks and hydrophobic contacts between the retinal-binding pocket and the cytoplasmic surface.
Figure 6.
Figure 6. Environment of the 11-cis-retinal. (a) Environment of the protonated Schiff base and its counterion Glu113. (b) Environment of the ionone ring and the kinks in H6 and H7 cross-linked by a water molecule.
The above figures are reproduced from the cited reference with permission from Elsevier
Secondary reference #2
Title Crystals of native and modified bovine rhodopsins and their heavy atom derivatives.
Authors P.C.Edwards, J.Li, M.Burghammer, J.H.Mcdowell, C.Villa, P.A.Hargrave, G.F.Schertler.
Ref. J Mol Biol, 2004, 343, 1439-1450. [DOI no: 10.1016/j.jmb.2004.08.089]
PubMed id 15491622
Full text Abstract
Figure 5.
Figure 5. Packing arrangement in the P31 crystal of native rhodopsin. (a) Two molecules in the asymmetric unit viewed along the non-crystallographic 2-fold axis, which passes between the pair of helices 5, one from each molecule, in an antiparallel orientation. (b) The same molecules rotated with the top towards the viewer by 908 about a horizontal line. Note the close approach between helices 5 along their entire length. The non-crystallographic 2-fold parallel with the c-axis (needle axis) of the crystal is now vertical. The C a trace is coloured in the rainbow order: H1, dark blue; H2, light blue; H3, cyan; H4, green; H5, yellow; H6, orange; H7, red; H8, magenta. (c) Stacking of helix bundles in side view. Single molecules are shown in different colours. Critical C 8E4 molecules are visible wedged between helices of neighbouring molecules. (d) Stacks of helix bundles in top view. Note the prominent hydrophilic water channel. The cytoplasmic and extracellular loops protrude undisturbed into this channel. The P31 packing retains an amphiphilic character similar to the environment in a membrane.
The above figure is reproduced from the cited reference with permission from Elsevier
PROCHECK
Go to PROCHECK summary
 Headers

 

spacer

spacer