1gmj

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{{STRUCTURE_1gmj| PDB=1gmj | SCENE= }}
{{STRUCTURE_1gmj| PDB=1gmj | SCENE= }}
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'''THE STRUCTURE OF BOVINE IF1, THE REGULATORY SUBUNIT OF MITOCHONDRIAL F-ATPASE'''
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===THE STRUCTURE OF BOVINE IF1, THE REGULATORY SUBUNIT OF MITOCHONDRIAL F-ATPASE===
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==Overview==
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In mitochondria, the hydrolytic activity of ATP synthase is regulated by an inhibitor protein, IF(1). Its binding to ATP synthase depends on pH, and below neutrality, IF(1) is dimeric and forms a stable complex with the enzyme. At higher pH values, IF(1) forms tetramers and is inactive. In the 2.2 A structure of the bovine IF(1) described here, the four monomers in the asymmetric unit are arranged as a dimer of dimers. Monomers form dimers via an antiparallel alpha-helical coiled coil in the C-terminal region. Dimers are associated into oligomers and form long fibres in the crystal lattice, via coiled-coil interactions in the N-terminal and inhibitory regions (residues 14-47). Therefore, tetramer formation masks the inhibitory region, preventing IF(1) binding to ATP synthase.
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(as it appears on PubMed at http://www.pubmed.gov), where 11742976 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11742976}}
==About this Structure==
==About this Structure==
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[[Category: Coiled-coil structure]]
[[Category: Coiled-coil structure]]
[[Category: P dependent oligomerization]]
[[Category: P dependent oligomerization]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:45:12 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 05:31:13 2008''

Revision as of 02:31, 1 July 2008

Template:STRUCTURE 1gmj

THE STRUCTURE OF BOVINE IF1, THE REGULATORY SUBUNIT OF MITOCHONDRIAL F-ATPASE

Template:ABSTRACT PUBMED 11742976

About this Structure

1GMJ is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

The structure of bovine IF(1), the regulatory subunit of mitochondrial F-ATPase., Cabezon E, Runswick MJ, Leslie AG, Walker JE, EMBO J. 2001 Dec 17;20(24):6990-6. PMID:11742976

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