1JJ7
Crystal Structure of the C-terminal ATPase domain of human TAP1
Summary for 1JJ7
| Entry DOI | 10.2210/pdb1jj7/pdb |
| Descriptor | PEPTIDE TRANSPORTER TAP1, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total) |
| Functional Keywords | p-loop, abc atpase domain, helical domain, protein transport |
| Biological source | Homo sapiens (human) |
| Cellular location | Endoplasmic reticulum membrane; Multi-pass membrane protein: Q03518 |
| Total number of polymer chains | 1 |
| Total formula weight | 28580.29 |
| Authors | Gaudet, R.,Wiley, D.C. (deposition date: 2001-07-03, release date: 2001-09-12, Last modification date: 2023-08-16) |
| Primary citation | Gaudet, R.,Wiley, D.C. Structure of the ABC ATPase domain of human TAP1, the transporter associated with antigen processing. EMBO J., 20:4964-4972, 2001 Cited by PubMed Abstract: 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. PubMed: 11532960DOI: 10.1093/emboj/20.17.4964 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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