2ixf

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[[Image:2ixf.gif|left|200px]]<br /><applet load="2ixf" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2ixf.gif|left|200px]]
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caption="2ixf, resolution 2.00&Aring;" />
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'''CRYSTAL STRUCTURE OF THE ATPASE DOMAIN OF TAP1 WITH ATP (D645Q, Q678H MUTANT)'''<br />
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{{Structure
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|PDB= 2ixf |SIZE=350|CAPTION= <scene name='initialview01'>2ixf</scene>, resolution 2.00&Aring;
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|SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+D'>AC1</scene>
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF THE ATPASE DOMAIN OF TAP1 WITH ATP (D645Q, Q678H MUTANT)'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2IXF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=ATP:'>ATP</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+D'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IXF OCA].
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2IXF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IXF OCA].
==Reference==
==Reference==
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Distinct structural and functional properties of the ATPase sites in an asymmetric ABC transporter., Procko E, Ferrin-O'Connell I, Ng SL, Gaudet R, Mol Cell. 2006 Oct 6;24(1):51-62. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17018292 17018292]
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Distinct structural and functional properties of the ATPase sites in an asymmetric ABC transporter., Procko E, Ferrin-O'Connell I, Ng SL, Gaudet R, Mol Cell. 2006 Oct 6;24(1):51-62. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17018292 17018292]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
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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 17:57:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:34:37 2008''

Revision as of 15:34, 20 March 2008

Image:2ixf.gif


PDB ID 2ixf

Drag the structure with the mouse to rotate
, resolution 2.00Å
Sites:
Ligands: , and
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF THE ATPASE DOMAIN OF TAP1 WITH ATP (D645Q, Q678H MUTANT)


Overview

The ABC transporter associated with antigen processing (TAP) shuttles cytosolic peptides into the endoplasmic reticulum for loading onto class I MHC molecules. Transport is fueled by ATP binding and hydrolysis at two distinct cytosolic ATPase sites. One site comprises consensus motifs shared among most ABC transporters, while the second has substituted, degenerate motifs. Biochemical and crystallography experiments with a TAP cytosolic domain demonstrate that the consensus ATPase site has high catalytic activity and facilitates ATP-dependent dimerization of the cytosolic domains, which is an important conformational change during transport. In contrast, the degenerate site is defective in dimerization and ATP hydrolysis. Full-length TAP mutagenesis demonstrates the necessity for at least one consensus site, supporting our conclusion that the consensus site is the principal facilitator of substrate transport. Since asymmetry of the ATPase site motifs is a feature of many mammalian homologs, our proposed model has broad implications for ABC transporters.

About this Structure

2IXF is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Distinct structural and functional properties of the ATPase sites in an asymmetric ABC transporter., Procko E, Ferrin-O'Connell I, Ng SL, Gaudet R, Mol Cell. 2006 Oct 6;24(1):51-62. PMID:17018292

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