1bmf: Difference between revisions

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[[Image:1bmf.gif|left|200px]]<br /><applet load="1bmf" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1bmf.gif|left|200px]]
caption="1bmf, resolution 2.85&Aring;" />
 
'''BOVINE MITOCHONDRIAL F1-ATPASE'''<br />
{{Structure
|PDB= 1bmf |SIZE=350|CAPTION= <scene name='initialview01'>1bmf</scene>, resolution 2.85&Aring;
|SITE= <scene name='pdbsite=CAT:The+Carboxylate+Group+Of+GLU+Residue+Is+Believed+To+Acti+...'>CAT</scene> and <scene name='pdbsite=PLP:LYS+Within+The+P-Loop+(Phosphate+Binding)+Motif,+Gxxxxgkt/S'>PLP</scene>
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene> and <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Transferred_entry:_3.6.3.14 Transferred entry: 3.6.3.14], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.34 3.6.1.34]
|GENE=
}}
 
'''BOVINE MITOCHONDRIAL F1-ATPASE'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1BMF is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=ANP:'>ANP</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Transferred_entry:_3.6.3.14 Transferred entry: 3.6.3.14], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.34 3.6.1.34] Known structural/functional Sites: <scene name='pdbsite=CAT:The+Carboxylate+Group+Of+GLU+Residue+Is+Believed+To+Acti+...'>CAT</scene> and <scene name='pdbsite=PLP:LYS+Within+The+P-Loop+(Phosphate+Binding)+Motif,+Gxxxxgkt/S'>PLP</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BMF OCA].  
1BMF is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BMF OCA].  


==Reference==
==Reference==
Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria., Abrahams JP, Leslie AG, Lutter R, Walker JE, Nature. 1994 Aug 25;370(6491):621-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8065448 8065448]
Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria., Abrahams JP, Leslie AG, Lutter R, Walker JE, Nature. 1994 Aug 25;370(6491):621-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8065448 8065448]
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: f1fo atp synthase]]
[[Category: f1fo atp synthase]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:56:48 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:12:57 2008''

Revision as of 11:12, 20 March 2008

File:1bmf.gif


PDB ID 1bmf

Drag the structure with the mouse to rotate
, resolution 2.85Å
Sites: and
Ligands: , and
Activity: Transferred entry: 3.6.3.14, with EC number 3.6.1.34
Coordinates: save as pdb, mmCIF, xml



BOVINE MITOCHONDRIAL F1-ATPASE


OverviewOverview

In the crystal structure of bovine mitochondrial F1-ATPase determined at 2.8 A resolution, the three catalytic beta-subunits differ in conformation and in the bound nucleotide. The structure supports a catalytic mechanism in intact ATP synthase in which the three catalytic subunits are in different states of the catalytic cycle at any instant. Interconversion of the states may be achieved by rotation of the alpha 3 beta 3 subassembly relative to an alpha-helical domain of the gamma-subunit.

About this StructureAbout this Structure

1BMF is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.

ReferenceReference

Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria., Abrahams JP, Leslie AG, Lutter R, Walker JE, Nature. 1994 Aug 25;370(6491):621-8. PMID:8065448

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