2hld: Difference between revisions

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[[Image:2hld.gif|left|200px]]<br /><applet load="2hld" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2hld.gif|left|200px]]
caption="2hld, resolution 2.80&Aring;" />
 
'''Crystal structure of yeast mitochondrial F1-ATPase'''<br />
{{Structure
|PDB= 2hld |SIZE=350|CAPTION= <scene name='initialview01'>2hld</scene>, resolution 2.80&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> and <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER'>ANP</scene>
|ACTIVITY= [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]
|GENE= ATP2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
}}
 
'''Crystal structure of yeast mitochondrial F1-ATPase'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
2HLD is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=ANP:'>ANP</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=2HLD OCA].  
2HLD is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HLD OCA].  


==Reference==
==Reference==
Novel features of the rotary catalytic mechanism revealed in the structure of yeast F1 ATPase., Kabaleeswaran V, Puri N, Walker JE, Leslie AG, Mueller DM, EMBO J. 2006 Nov 15;25(22):5433-42. Epub 2006 Nov 2. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17082766 17082766]
Novel features of the rotary catalytic mechanism revealed in the structure of yeast F1 ATPase., Kabaleeswaran V, Puri N, Walker JE, Leslie AG, Mueller DM, EMBO J. 2006 Nov 15;25(22):5433-42. Epub 2006 Nov 2. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17082766 17082766]
[[Category: H(+)-transporting two-sector ATPase]]
[[Category: H(+)-transporting two-sector ATPase]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: f1fo]]
[[Category: f1fo]]


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Revision as of 18:18, 20 March 2008

File:2hld.gif


PDB ID 2hld

Drag the structure with the mouse to rotate
, resolution 2.80Å
Ligands: , and
Gene: ATP2 (Saccharomyces cerevisiae)
Activity: H(+)-transporting two-sector ATPase, with EC number 3.6.3.14
Coordinates: save as pdb, mmCIF, xml



Crystal structure of yeast mitochondrial F1-ATPase


OverviewOverview

The crystal structure of yeast mitochondrial F(1) ATPase contains three independent copies of the complex, two of which have similar conformations while the third differs in the position of the central stalk relative to the alpha(3)beta(3) sub-assembly. All three copies display very similar asymmetric features to those observed for the bovine enzyme, but the yeast F(1) ATPase structures provide novel information. In particular, the active site that binds ADP in bovine F(1) ATPase has an ATP analog bound and therefore this structure does not represent the ADP-inhibited form. In addition, one of the complexes binds phosphate in the nucleotide-free catalytic site, and comparison with other structures provides a picture of the movement of the phosphate group during initial binding and subsequent catalysis. The shifts in position of the central stalk between two of the three copies of yeast F(1) ATPase and when these structures are compared to those of the bovine enzyme give new insight into the conformational changes that take place during rotational catalysis.

About this StructureAbout this Structure

2HLD is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

Novel features of the rotary catalytic mechanism revealed in the structure of yeast F1 ATPase., Kabaleeswaran V, Puri N, Walker JE, Leslie AG, Mueller DM, EMBO J. 2006 Nov 15;25(22):5433-42. Epub 2006 Nov 2. PMID:17082766

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