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 2.8&Aring;" /> '''RAT LIVER F1-ATPASE''...)
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[[Image:1mab.jpg|left|200px]]<br /><applet load="1mab" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1mab.jpg|left|200px]]<br /><applet load="1mab" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1mab, resolution 2.8&Aring;" />
caption="1mab, resolution 2.8&Aring;" />
'''RAT LIVER F1-ATPASE'''<br />
'''RAT LIVER F1-ATPASE'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1MAB is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with PO4, MG, ATP and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MAB OCA].
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1MAB is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=PO4:'>PO4</scene>, <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=ATP:'>ATP</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MAB OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Amzel, L.M.]]
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[[Category: Amzel, L M.]]
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[[Category: Bianchet, M.A.]]
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[[Category: Bianchet, M A.]]
[[Category: ADP]]
[[Category: ADP]]
[[Category: ATP]]
[[Category: ATP]]
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[[Category: oxidative phosphorylation]]
[[Category: oxidative phosphorylation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:16:20 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:53:11 2008''

Revision as of 11:53, 21 February 2008


1mab, resolution 2.8Å

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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 , , and 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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