1xp5

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[[Image:1xp5.gif|left|200px]]<br /><applet load="1xp5" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1xp5.gif|left|200px]]
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caption="1xp5, resolution 3.0&Aring;" />
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'''Structure Of The (Sr)Ca2+-ATPase E2-AlF4- Form'''<br />
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{{Structure
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|PDB= 1xp5 |SIZE=350|CAPTION= <scene name='initialview01'>1xp5</scene>, resolution 3.0&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene> and <scene name='pdbligand=TG1:OCTANOIC ACID [3S-[3ALPHA, 3ABETA, 4ALPHA, 6BETA, 6ABETA, 7BETA, 8ALPHA(Z), 9BALPHA]]-6-(ACETYLOXY)-2,3,-3A,4,5,6,6A,7,8,9B-DECAHYDRO-3,3A-DIHYDROXY-3,6,9-TRIMETHYL-8-[(2-METHYL-1-OXO-2-BUTENYL)OXY]-2-OXO-4-(1-OXOBUTOXY)-AZULENO[4,5-B]FURAN-7-YL ESTER'>TG1</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''Structure Of The (Sr)Ca2+-ATPase E2-AlF4- Form'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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1XP5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XP5 OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15618517 15618517]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15618517 15618517]
[[Category: Calcium-transporting ATPase]]
[[Category: Calcium-transporting ATPase]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
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[[Category: p-type atpase]]
[[Category: p-type atpase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:57:11 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:12:43 2008''

Revision as of 13:12, 20 March 2008


PDB ID 1xp5

Drag the structure with the mouse to rotate
, resolution 3.0Å
Ligands: , , and
Activity: Calcium-transporting ATPase, with EC number 3.6.3.8
Coordinates: save as pdb, mmCIF, xml



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. 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

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