2ixf | pdb_00002ixf
CRYSTAL STRUCTURE OF THE ATPASE DOMAIN OF TAP1 WITH ATP (D645Q, Q678H MUTANT)
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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 ... [(full description)]
About this Structure
2IXF is a [Single protein] structure of sequence from [Rattus norvegicus] with MG, ATP and GOL as [ligands]. 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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