1jj7
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(New page: 200px<br /> <applet load="1jj7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jj7, resolution 2.40Å" /> '''Crystal Structure o...)
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Revision as of 15:34, 12 November 2007
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Crystal Structure of the C-terminal ATPase domain of human TAP1
Overview
The transporter associated with antigen processing (TAP) is an ABC, transporter formed of two subunits, TAP1 and TAP2, each of which has an, N-terminal membrane-spanning domain and a C-terminal ABC ATPase domain. We, report the structure of the C-terminal ABC ATPase domain of TAP1 (cTAP1), bound to ADP. cTAP1 forms an L-shaped molecule with two domains, a, RecA-like domain and a small alpha-helical domain. The diphosphate group, of ADP interacts with the P-loop as expected. Residues thought to be, involved in gamma-phosphate binding and hydrolysis show flexibility in the, ADP-bound state as evidenced by their high B-factors. Comparisons of cTAP1, with other ABC ATPases from the ABC transporter family as well as ABC, ATPases involved in DNA maintenance and repair reveal key regions and, residues specific to each family. Three ATPase subfamilies are identified, which have distinct adenosine recognition motifs, as well as distinct, subdomains that may be specific to the different functions of each, subfamily. Differences between TAP1 and TAP2 in the nucleotide-binding, site may be related to the observed asymmetry during peptide transport.
About this Structure
1JJ7 is a Single protein structure of sequence from Homo sapiens with MG and ADP as ligands. Full crystallographic information is available from OCA.
Reference
Structure of the ABC ATPase domain of human TAP1, the transporter associated with antigen processing., Gaudet R, Wiley DC, EMBO J. 2001 Sep 3;20(17):4964-72. PMID:11532960
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Categories: Homo sapiens | Single protein | Gaudet, R. | Wiley, D.C. | ADP | MG | Abc atpase domain | Helical domain | P-loop