1c17

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1c17.gif|left|200px]]
+
[[Image:1c17.png|left|200px]]
<!--
<!--
Line 12: Line 12:
-
==Overview==
+
{{ABSTRACT_10580496}}
-
F1F0 ATP synthases use a transmembrane proton gradient to drive the synthesis of cellular ATP. The structure of the cytosolic F1 portion of the enzyme and the basic mechanism of ATP hydrolysis by F1 are now well established, but how proton translocation through the transmembrane F0 portion drives these catalytic changes is less clear. Here we describe the structural changes in the proton-translocating F0 subunit c that are induced by deprotonating the specific aspartic acid involved in proton transport. Conformational changes between the protonated and deprotonated forms of subunit c provide the structural basis for an explicit mechanism to explain coupling of proton translocation by F0 to the rotation of subunits within the core of F1. Rotation of these subunits within F1 causes the catalytic conformational changes in the active sites of F1 that result in ATP synthesis.
+
==About this Structure==
==About this Structure==
1C17 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. The following page contains interesting information on the relation of 1C17 with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb72_1.html ATP Synthase]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C17 OCA].
1C17 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. The following page contains interesting information on the relation of 1C17 with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb72_1.html ATP Synthase]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C17 OCA].
- 
-
==Reference==
 
-
Structural changes linked to proton translocation by subunit c of the ATP synthase., Rastogi VK, Girvin ME, Nature. 1999 Nov 18;402(6759):263-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10580496 10580496]
 
[[Category: ATP Synthase]]
[[Category: ATP Synthase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
Line 28: Line 24:
[[Category: Helix]]
[[Category: Helix]]
[[Category: Membrane protein]]
[[Category: Membrane protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:12:39 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jun 26 17:06:14 2008''

Revision as of 14:06, 26 June 2008

Template:STRUCTURE 1c17

A1C12 SUBCOMPLEX OF F1FO ATP SYNTHASE


Template:ABSTRACT 10580496

About this Structure

1C17 is a Protein complex structure of sequences from Escherichia coli. The following page contains interesting information on the relation of 1C17 with [ATP Synthase]. Full crystallographic information is available from OCA.

Page seeded by OCA on Thu Jun 26 17:06:14 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools