2c61: Difference between revisions

Revision as of 17:45, 21 February 2008

CRYSTAL STRUCTURE OF THE NON-CATALYTIC B SUBUNIT OF A-TYPE ATPASE FROM M. MAZEI GO1

OverviewOverview

The A1Ao ATP synthase from archaea represents a class of chimeric ATPases/synthases, whose function and general structural design share characteristics both with vacuolar V1Vo ATPases and with F1Fo ATP synthases. The primary sequences of the two large polypeptides A and B, from the catalytic part, are closely related to the eukaryotic V1Vo ATPases. The chimeric nature of the A1Ao ATP synthase from the archaeon Methanosarcina mazei Go1 was investigated in terms of nucleotide interaction. Here, we demonstrate the ability of the overexpressed A and B subunits to bind ADP and ATP by photoaffinity labeling. Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry was used to map the peptide of subunit B involved in nucleotide interaction. Nucleotide affinities in both subunits were determined by fluorescence correlation spectroscopy, indicating a weaker binding of nucleotide analogues to subunit B than to A. In addition, the nucleotide-free crystal structure of subunit B is presented at 1.5 A resolution, providing the first view of the so-called non-catalytic subunit of the A1Ao ATP synthase. Superposition of the A-ATP synthase non-catalytic B subunit and the F-ATP synthase non-catalytic alpha subunit provides new insights into the similarities and differences of these nucleotide-binding ATPase subunits in particular, and into nucleotide binding in general. The arrangement of subunit B within the intact A1Ao ATP synthase is presented.

About this StructureAbout this Structure

2C61 is a Single protein structure of sequence from Methanosarcina mazei go1. Active as H(+)-transporting two-sector ATPase, with EC number 3.6.3.14 Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the archaeal A1Ao ATP synthase subunit B from Methanosarcina mazei Go1: Implications of nucleotide-binding differences in the major A1Ao subunits A and B., Schafer IB, Bailer SM, Duser MG, Borsch M, Bernal RA, Stock D, Gruber G, J Mol Biol. 2006 May 5;358(3):725-40. Epub 2006 Mar 10. PMID:16563431

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 ==Overview==
-The A1Ao ATP synthase from archaea represents a class of chimeric, ATPases/synthases, whose function and general structural design share, characteristics both with vacuolar V1Vo ATPases and with F1Fo ATP, synthases. The primary sequences of the two large polypeptides A and B, from the catalytic part, are closely related to the eukaryotic V1Vo, ATPases. The chimeric nature of the A1Ao ATP synthase from the archaeon, Methanosarcina mazei Go1 was investigated in terms of nucleotide, interaction. Here, we demonstrate the ability of the overexpressed A and B, subunits to bind ADP and ATP by photoaffinity labeling. Matrix-assisted, laser desorption/ionization time-of-flight mass spectrometry was used to, map the peptide of subunit B involved in nucleotide interaction., Nucleotide affinities in both subunits were determined by fluorescence, correlation spectroscopy, indicating a weaker binding of nucleotide, analogues to subunit B than to A. In addition, the nucleotide-free crystal, structure of subunit B is presented at 1.5 A resolution, providing the, first view of the so-called non-catalytic subunit of the A1Ao ATP, synthase. Superposition of the A-ATP synthase non-catalytic B subunit and, the F-ATP synthase non-catalytic alpha subunit provides new insights into, the similarities and differences of these nucleotide-binding ATPase, subunits in particular, and into nucleotide binding in general. The, arrangement of subunit B within the intact A1Ao ATP synthase is presented.
+The A1Ao ATP synthase from archaea represents a class of chimeric ATPases/synthases, whose function and general structural design share characteristics both with vacuolar V1Vo ATPases and with F1Fo ATP synthases. The primary sequences of the two large polypeptides A and B, from the catalytic part, are closely related to the eukaryotic V1Vo ATPases. The chimeric nature of the A1Ao ATP synthase from the archaeon Methanosarcina mazei Go1 was investigated in terms of nucleotide interaction. Here, we demonstrate the ability of the overexpressed A and B subunits to bind ADP and ATP by photoaffinity labeling. Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry was used to map the peptide of subunit B involved in nucleotide interaction. Nucleotide affinities in both subunits were determined by fluorescence correlation spectroscopy, indicating a weaker binding of nucleotide analogues to subunit B than to A. In addition, the nucleotide-free crystal structure of subunit B is presented at 1.5 A resolution, providing the first view of the so-called non-catalytic subunit of the A1Ao ATP synthase. Superposition of the A-ATP synthase non-catalytic B subunit and the F-ATP synthase non-catalytic alpha subunit provides new insights into the similarities and differences of these nucleotide-binding ATPase subunits in particular, and into nucleotide binding in general. The arrangement of subunit B within the intact A1Ao ATP synthase is presented.
 ==About this Structure==
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 [[Category: Methanosarcina mazei go1]]
 [[Category: Single protein]]
-[[Category: Bailer, S.M.]]
+[[Category: Bailer, S M.]]
-[[Category: Bernal, R.A.]]
+[[Category: Bernal, R A.]]
 [[Category: Boersch, M.]]
 [[Category: Dueser, M.]]
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 [[Category: transport]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 18:37:06 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:45:16 2008''