1mab
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(New page: 200px<br /><applet load="1mab" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mab, resolution 2.8Å" /> '''RAT LIVER F1-ATPASE''...)
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Revision as of 19:09, 20 November 2007
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RAT LIVER F1-ATPASE
Overview
During mitochondrial ATP synthesis, F1-ATPase-the portion of the ATP, synthase that contains the catalytic and regulatory nucleotide binding, sites-undergoes a series of concerted conformational changes that couple, proton translocation to the synthesis of the high levels of ATP required, for cellular function. In the structure of the rat liver F1-ATPase, determined to 2.8-A resolution in the presence of physiological, concentrations of nucleotides, all three beta subunits contain bound, nucleotide and adopt similar conformations. This structure provides the, missing configuration of F1 necessary to define all intermediates in the, reaction pathway. Incorporation of this structure suggests a mechanism of, ATP synthesis/hydrolysis in which configurations of the enzyme with three, bound nucleotides play an essential role.
About this Structure
1MAB is a Protein complex structure of sequences from Rattus norvegicus with PO4, MG, ATP and ADP as ligands. Active as H(+)-transporting two-sector ATPase, with EC number 3.6.3.14 Full crystallographic information is available from OCA.
Reference
The 2.8-A structure of rat liver F1-ATPase: configuration of a critical intermediate in ATP synthesis/hydrolysis., Bianchet MA, Hullihen J, Pedersen PL, Amzel LM, Proc Natl Acad Sci U S A. 1998 Sep 15;95(19):11065-70. PMID:9736690
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