1xp5
From Proteopedia
(New page: 200px<br /><applet load="1xp5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xp5, resolution 3.0Å" /> '''Structure Of The (Sr)...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1xp5.gif|left|200px]]<br /><applet load="1xp5" size=" | + | [[Image:1xp5.gif|left|200px]]<br /><applet load="1xp5" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1xp5, resolution 3.0Å" /> | caption="1xp5, resolution 3.0Å" /> | ||
'''Structure Of The (Sr)Ca2+-ATPase E2-AlF4- Form'''<br /> | '''Structure Of The (Sr)Ca2+-ATPase E2-AlF4- Form'''<br /> | ||
==Overview== | ==Overview== | ||
| - | P-type ATPases extract energy by hydrolysis of adenosine triphosphate | + | P-type ATPases extract energy by hydrolysis of adenosine triphosphate (ATP) in two steps, formation and breakdown of a covalent phosphoenzyme intermediate. This process drives active transport and countertransport of the cation pumps. We have determined the crystal structure of rabbit sarcoplasmic reticulum Ca2+ adenosine triphosphatase in complex with aluminum fluoride, which mimics the transition state of hydrolysis of the counterion-bound (protonated) phosphoenzyme. On the basis of structural analysis and biochemical data, we find this form to represent an occluded state of the proton counterions. Hydrolysis is catalyzed by the conserved Thr-Gly-Glu-Ser motif, and it exploits an associative nucleophilic reaction mechanism of the same type as phosphoryl transfer from ATP. On this basis, we propose a general mechanism of occluded transition states of Ca2+ transport and H+ countertransport coupled to phosphorylation and dephosphorylation, respectively. |
==About this Structure== | ==About this Structure== | ||
| - | 1XP5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with MG, ALF, K and TG1 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Calcium-transporting_ATPase Calcium-transporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.8 3.6.3.8] Full crystallographic information is available from [http:// | + | 1XP5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=ALF:'>ALF</scene>, <scene name='pdbligand=K:'>K</scene> and <scene name='pdbligand=TG1:'>TG1</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Calcium-transporting_ATPase Calcium-transporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.8 3.6.3.8] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XP5 OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Moller, J | + | [[Category: Moller, J V.]] |
| - | [[Category: Nielsen, R | + | [[Category: Nielsen, R C.]] |
[[Category: Nissen, P.]] | [[Category: Nissen, P.]] | ||
[[Category: Olesen, C.]] | [[Category: Olesen, C.]] | ||
| - | [[Category: Sorensen, T | + | [[Category: Sorensen, T L.S.]] |
[[Category: ALF]] | [[Category: ALF]] | ||
[[Category: K]] | [[Category: K]] | ||
| Line 28: | Line 28: | ||
[[Category: p-type atpase]] | [[Category: p-type atpase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:57:11 2008'' |
Revision as of 13:57, 21 February 2008
|
Structure Of The (Sr)Ca2+-ATPase E2-AlF4- Form
Overview
P-type ATPases extract energy by hydrolysis of adenosine triphosphate (ATP) in two steps, formation and breakdown of a covalent phosphoenzyme intermediate. This process drives active transport and countertransport of the cation pumps. We have determined the crystal structure of rabbit sarcoplasmic reticulum Ca2+ adenosine triphosphatase in complex with aluminum fluoride, which mimics the transition state of hydrolysis of the counterion-bound (protonated) phosphoenzyme. On the basis of structural analysis and biochemical data, we find this form to represent an occluded state of the proton counterions. Hydrolysis is catalyzed by the conserved Thr-Gly-Glu-Ser motif, and it exploits an associative nucleophilic reaction mechanism of the same type as phosphoryl transfer from ATP. On this basis, we propose a general mechanism of occluded transition states of Ca2+ transport and H+ countertransport coupled to phosphorylation and dephosphorylation, respectively.
About this Structure
1XP5 is a Single protein structure of sequence from Oryctolagus cuniculus with , , and as ligands. Active as Calcium-transporting ATPase, with EC number 3.6.3.8 Full crystallographic information is available from OCA.
Reference
Dephosphorylation of the calcium pump coupled to counterion occlusion., Olesen C, Sorensen TL, Nielsen RC, Moller JV, Nissen P, Science. 2004 Dec 24;306(5705):2251-5. PMID:15618517
Page seeded by OCA on Thu Feb 21 15:57:11 2008
