We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1cwq

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1cwq.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1cwq.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1cwq| PDB=1cwq | SCENE= }}
{{STRUCTURE_1cwq| PDB=1cwq | SCENE= }}
-
'''M INTERMEDIATE STRUCTURE OF THE WILD TYPE BACTERIORHODOPSIN IN COMBINATION WITH THE GROUND STATE STRUCTURE'''
+
===M INTERMEDIATE STRUCTURE OF THE WILD TYPE BACTERIORHODOPSIN IN COMBINATION WITH THE GROUND STATE STRUCTURE===
-
==Overview==
+
<!--
-
The transport of protons across membranes is an important process in cellular bioenergetics. The light-driven proton pump bacteriorhodopsin is the best-characterized protein providing this function. Photon energy is absorbed by the chromophore retinal, covalently bound to Lys 216 via a protonated Schiff base. The light-induced all-trans to 13-cis isomerization of the retinal results in deprotonation of the Schiff base followed by alterations in protonatable groups within bacteriorhodopsin. The changed force field induces changes, even in the tertiary structure, which are necessary for proton pumping. The recent report of a high-resolution X-ray crystal structure for the late M intermediate of a mutant bacteriorhopsin (with Asp 96--&gt;Asn) displays the structure of a proton pathway highly disturbed by the mutation. To observe an unperturbed proton pathway, we determined the structure of the late M intermediate of wild-type bacteriorhodopsin (2.25 A resolution). The cytoplasmic side of our M2 structure shows a water net that allows proton transfer from the proton donor group Asp 96 towards the Schiff base. An enlarged cavity system above Asp 96 is observed, which facilitates the de- and reprotonation of this group by fluctuating water molecules in the last part of the cycle.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10949308}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10949308 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10949308}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Proton transport]]
[[Category: Proton transport]]
[[Category: Retinal protein]]
[[Category: Retinal protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:11:33 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 21:39:06 2008''

Revision as of 18:39, 30 June 2008

Image:1cwq.png

Template:STRUCTURE 1cwq

M INTERMEDIATE STRUCTURE OF THE WILD TYPE BACTERIORHODOPSIN IN COMBINATION WITH THE GROUND STATE STRUCTURE

Template:ABSTRACT PUBMED 10949308

About this Structure

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

Reference

Structural alterations for proton translocation in the M state of wild-type bacteriorhodopsin., Sass HJ, Buldt G, Gessenich R, Hehn D, Neff D, Schlesinger R, Berendzen J, Ormos P, Nature. 2000 Aug 10;406(6796):649-53. PMID:10949308

Page seeded by OCA on Mon Jun 30 21:39:06 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1cwq"
Personal tools