1mhs
From Proteopedia
(New page: 200px<br /><applet load="1mhs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mhs, resolution 8.0Å" /> '''Model of Neurospora c...) |
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| - | [[Image:1mhs.gif|left|200px]]<br /><applet load="1mhs" size=" | + | [[Image:1mhs.gif|left|200px]]<br /><applet load="1mhs" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1mhs, resolution 8.0Å" /> | caption="1mhs, resolution 8.0Å" /> | ||
'''Model of Neurospora crassa proton ATPase'''<br /> | '''Model of Neurospora crassa proton ATPase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Proton pumps in the plasma membrane of plants and yeasts maintain the | + | Proton pumps in the plasma membrane of plants and yeasts maintain the intracellular pH and membrane potential. To gain insight into the molecular mechanisms of proton pumping, we built an atomic homology model of the proton pump based on the 2.6 angstrom x-ray structure of the related Ca2+ pump from rabbit sarcoplasmic reticulum. The model, when fitted to an 8 angstrom map of the Neurospora proton pump determined by electron microscopy, reveals the likely path of the proton through the membrane and shows that the nucleotide-binding domain rotates by approximately 70 degrees to deliver adenosine triphosphate (ATP) to the phosphorylation site. A synthetic peptide corresponding to the carboxyl-terminal regulatory domain stimulates ATPase activity, suggesting a mechanism for proton transport regulation. |
==About this Structure== | ==About this Structure== | ||
| - | 1MHS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Neurospora_crassa Neurospora crassa]. Active as [http://en.wikipedia.org/wiki/Proton-exporting_ATPase Proton-exporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.6 3.6.3.6] Full crystallographic information is available from [http:// | + | 1MHS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Neurospora_crassa Neurospora crassa]. Active as [http://en.wikipedia.org/wiki/Proton-exporting_ATPase Proton-exporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.6 3.6.3.6] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MHS OCA]. |
==Reference== | ==Reference== | ||
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[[Category: proton pump]] | [[Category: proton pump]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:55:18 2008'' |
Revision as of 11:55, 21 February 2008
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Model of Neurospora crassa proton ATPase
Overview
Proton pumps in the plasma membrane of plants and yeasts maintain the intracellular pH and membrane potential. To gain insight into the molecular mechanisms of proton pumping, we built an atomic homology model of the proton pump based on the 2.6 angstrom x-ray structure of the related Ca2+ pump from rabbit sarcoplasmic reticulum. The model, when fitted to an 8 angstrom map of the Neurospora proton pump determined by electron microscopy, reveals the likely path of the proton through the membrane and shows that the nucleotide-binding domain rotates by approximately 70 degrees to deliver adenosine triphosphate (ATP) to the phosphorylation site. A synthetic peptide corresponding to the carboxyl-terminal regulatory domain stimulates ATPase activity, suggesting a mechanism for proton transport regulation.
About this Structure
1MHS is a Single protein structure of sequence from Neurospora crassa. Active as Proton-exporting ATPase, with EC number 3.6.3.6 Full crystallographic information is available from OCA.
Reference
Structure, mechanism, and regulation of the Neurospora plasma membrane H+-ATPase., Kuhlbrandt W, Zeelen J, Dietrich J, Science. 2002 Sep 6;297(5587):1692-6. Epub 2002 Aug 8. PMID:12169656
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