1vzs
From Proteopedia
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SOLUTION STRUCTURE OF SUBUNIT F6 FROM THE PERIPHERAL STALK REGION OF ATP SYNTHASE FROM BOVINE HEART MITOCHONDRIA
Overview
The ATP synthase enzyme structure includes two stalk assemblies, the, central stalk and the peripheral stalk. Catalysis involves rotation of the, central stalk assembly together with the membrane-embedded ring of, c-subunits driven by the trans-membrane proton-motive force, while the, alpha and beta-subunits of F(1) are prevented from co-rotating by their, attachment to the peripheral stalk. In the absence of structures of either, the intact peripheral stalk or larger complexes containing it, we are, studying its individual components and their interactions to build up an, overall picture of its structure. Here, we describe an NMR structural, characterisation of F(6), which is a 76-residue protein located in the, peripheral stalk of the bovine ATP synthase and is essential for coupling, between the proton-motive force and catalysis. Isolated F(6) has a highly, flexible structure comprising two helices packed together through a loose, hydrophobic core and connected by an unstructured linker. Analysis of, chemical shifts, (15)N relaxation and RDC measurements confirm that the, F(6) structure is flexible on a wide range of timescales ranging from, nanoseconds to seconds. The relationship between this structure for, isolated F(6) and its role in the intact peripheral stalk is discussed.
About this Structure
1VZS is a Single protein structure of sequence from Bos taurus. Active as H(+)-transporting two-sector ATPase, with EC number 3.6.3.14 Full crystallographic information is available from OCA.
Reference
Solution structure of subunit F(6) from the peripheral stalk region of ATP synthase from bovine heart mitochondria., Carbajo RJ, Silvester JA, Runswick MJ, Walker JE, Neuhaus D, J Mol Biol. 2004 Sep 10;342(2):593-603. PMID:15327958
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