1bm1: Difference between revisions

Revision as of 19:22, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1bm1.png

Template:STRUCTURE 1bm1

CRYSTAL STRUCTURE OF BACTERIORHODOPSIN IN THE LIGHT-ADAPTED STATECRYSTAL STRUCTURE OF BACTERIORHODOPSIN IN THE LIGHT-ADAPTED STATE

Template:ABSTRACT PUBMED 10393291

About this StructureAbout this Structure

1BM1 is a Single protein structure of sequence from Halobacterium salinarum. Full crystallographic information is available from OCA.

ReferenceReference

Specific lipid-protein interactions in a novel honeycomb lattice structure of bacteriorhodopsin., Sato H, Takeda K, Tani K, Hino T, Okada T, Nakasako M, Kamiya N, Kouyama T, Acta Crystallogr D Biol Crystallogr. 1999 Jul;55(Pt 7):1251-6. PMID:10393291

Page seeded by OCA on Mon Jun 30 19:22:00 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1bm1.gif|left|200px]]
+{{Seed}}
+[[Image:1bm1.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1bm1|  PDB=1bm1  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF BACTERIORHODOPSIN IN THE LIGHT-ADAPTED STATE'''
+===CRYSTAL STRUCTURE OF BACTERIORHODOPSIN IN THE LIGHT-ADAPTED STATE===
-==Overview==
+<!--
-In the purple membrane of Halobacterium salinarium, bacteriorhodopsin trimers are arranged in a hexagonal lattice. When purple membrane sheets are incubated at high temperature with neutral detergent, membrane vesicularization takes place, yielding inside-out vesicles with a diameter of 50 nm. The vesicular structure becomes unstable at low temperature, where successive fusion of the vesicles yields a crystal which is composed of stacked planar membranes. X-ray crystallographic analysis reveals that the bacteriorhodopsin trimers are arranged in a honeycomb lattice in each membrane layer and that neighbouring membranes orient in opposite directions. The native structure of the trimeric unit is preserved in the honeycomb lattice, irrespective of alterations in the in-plane orientation of the trimer. One phospholipid tightly bound to a crevice between monomers in the trimeric unit is suggested to act as a glue in the formation of the trimer.
+The line below this paragraph, {{ABSTRACT_PUBMED_10393291}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10393291 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10393291}}
 ==About this Structure==
@@ Line 34: / Line 38: @@
 [[Category: Proton pump]]
 [[Category: Retinal protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 11:40:57 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:22:00 2008''