2ixf
From Proteopedia
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| - | [[Image:2ixf.gif|left|200px]]<br /><applet load="2ixf" size=" | + | [[Image:2ixf.gif|left|200px]]<br /><applet load="2ixf" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2ixf, resolution 2.00Å" /> | caption="2ixf, resolution 2.00Å" /> | ||
'''CRYSTAL STRUCTURE OF THE ATPASE DOMAIN OF TAP1 WITH ATP (D645Q, Q678H MUTANT)'''<br /> | '''CRYSTAL STRUCTURE OF THE ATPASE DOMAIN OF TAP1 WITH ATP (D645Q, Q678H MUTANT)'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 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 MG, ATP and GOL 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:// | + | 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]. |
==Reference== | ==Reference== | ||
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[[Category: transport]] | [[Category: transport]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:39:22 2008'' |
Revision as of 08:39, 3 February 2008
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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 with , and as ligands. Known structural/functional Site: . 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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Categories: Rattus norvegicus | Single protein | Connell, I.Ferrin-O. | Gaudet, R. | Ng, S.L. | Procko, E. | ATP | GOL | MG | Abc atpase | Atp-binding | Endoplasmic reticulum | Hydrolase | Immune response | Membrane | Nucleotide-binding | Peptide transport | Protein transport | Transmembrane | Transport
