2hld
From Proteopedia
(New page: 200px<br /><applet load="2hld" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hld, resolution 2.80Å" /> '''Crystal structure of...) |
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| - | [[Image:2hld.gif|left|200px]]<br /><applet load="2hld" size=" | + | [[Image:2hld.gif|left|200px]]<br /><applet load="2hld" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2hld, resolution 2.80Å" /> | caption="2hld, resolution 2.80Å" /> | ||
'''Crystal structure of yeast mitochondrial F1-ATPase'''<br /> | '''Crystal structure of yeast mitochondrial F1-ATPase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of yeast mitochondrial F(1) ATPase contains three | + | 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 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 MG, PO4 and ANP 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:// | + | 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]. |
==Reference== | ==Reference== | ||
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[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Kabaleeswaran, V.]] | [[Category: Kabaleeswaran, V.]] | ||
| - | [[Category: Leslie, A | + | [[Category: Leslie, A G.]] |
| - | [[Category: Mueller, D | + | [[Category: Mueller, D M.]] |
[[Category: Puri, N.]] | [[Category: Puri, N.]] | ||
| - | [[Category: Walker, J | + | [[Category: Walker, J E.]] |
[[Category: ANP]] | [[Category: ANP]] | ||
[[Category: MG]] | [[Category: MG]] | ||
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[[Category: f1fo]] | [[Category: f1fo]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:43:02 2008'' |
Revision as of 15:43, 21 February 2008
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Crystal structure of yeast mitochondrial F1-ATPase
Overview
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 Structure
2HLD is a Protein complex structure of sequences from Saccharomyces cerevisiae 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
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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