2ixe

From Proteopedia

Revision as of 10:52, 30 October 2007

CRYSTAL STRUCTURE OF THE ATPASE DOMAIN OF TAP1 WITH ATP (D645N 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 ... [(full description)]

About this Structure

2IXE is a [Single protein] structure of sequence from [Rattus norvegicus] with MG, PO4 and ATP as [ligands]. Structure known Active Site: AC1. 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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