2zbf

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[[Image:2zbf.jpg|left|200px]]<br /><applet load="2zbf" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2zbf.jpg|left|200px]]
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caption="2zbf, resolution 2.40&Aring;" />
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'''Calcium pump crystal structure with bound BeF3 and TG in the absence of calcium'''<br />
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{{Structure
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|PDB= 2zbf |SIZE=350|CAPTION= <scene name='initialview01'>2zbf</scene>, resolution 2.40&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</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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'''Calcium pump crystal structure with bound BeF3 and TG in the absence of calcium'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2ZBF 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=BEF:'>BEF</scene>, <scene name='pdbligand=ACE:'>ACE</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=2ZBF OCA].
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2ZBF 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=2ZBF OCA].
==Reference==
==Reference==
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How processing of aspartylphosphate is coupled to lumenal gating of the ion pathway in the calcium pump., Toyoshima C, Norimatsu Y, Iwasawa S, Tsuda T, Ogawa H, Proc Natl Acad Sci U S A. 2007 Dec 11;104(50):19831-6. Epub 2007 Dec 5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18077416 18077416]
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How processing of aspartylphosphate is coupled to lumenal gating of the ion pathway in the calcium pump., Toyoshima C, Norimatsu Y, Iwasawa S, Tsuda T, Ogawa H, Proc Natl Acad Sci U S A. 2007 Dec 11;104(50):19831-6. Epub 2007 Dec 5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18077416 18077416]
[[Category: Calcium-transporting ATPase]]
[[Category: Calcium-transporting ATPase]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
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[[Category: transport]]
[[Category: transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:01:20 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:53:46 2008''

Revision as of 16:53, 20 March 2008

Image:2zbf.jpg


PDB ID 2zbf

Drag the structure with the mouse to rotate
, resolution 2.40Å
Ligands: , , and
Activity: Calcium-transporting ATPase, with EC number 3.6.3.8
Coordinates: save as pdb, mmCIF, xml



Calcium pump crystal structure with bound BeF3 and TG in the absence of calcium


Overview

Ca(2+)-ATPase of skeletal muscle sarcoplasmic reticulum is the best-studied member of the P-type or E1/E2 type ion transporting ATPases. It has been crystallized in seven different states that cover nearly the entire reaction cycle. Here we describe the structure of this ATPase complexed with phosphate analogs BeF(3)(-) and AlF(4)(-) in the absence of Ca(2+), which correspond to the E2P ground state and E2 approximately P transition state, respectively. The luminal gate is open with BeF(3)(-) and closed with AlF(4)(-). These and the E1 approximately P.ADP analog crystal structures show that a two-step rotation of the cytoplasmic A-domain opens and closes the luminal gate through the movements of the M1-M4 transmembrane helices. There are several conformational switches coupled to the rotation, and the one in the cytoplasmic part of M2 has critical importance. In the second step of rotation, positioning of one water molecule couples the hydrolysis of aspartylphosphate to closing of the gate.

About this Structure

2ZBF is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.

Reference

How processing of aspartylphosphate is coupled to lumenal gating of the ion pathway in the calcium pump., Toyoshima C, Norimatsu Y, Iwasawa S, Tsuda T, Ogawa H, Proc Natl Acad Sci U S A. 2007 Dec 11;104(50):19831-6. Epub 2007 Dec 5. PMID:18077416

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