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1JJ7

Crystal Structure of the C-terminal ATPase domain of human TAP1

Summary for 1JJ7
Entry DOI10.2210/pdb1jj7/pdb
DescriptorPEPTIDE TRANSPORTER TAP1, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
Functional Keywordsp-loop, abc atpase domain, helical domain, protein transport
Biological sourceHomo sapiens (human)
Cellular locationEndoplasmic reticulum membrane; Multi-pass membrane protein: Q03518
Total number of polymer chains1
Total formula weight28580.29
Authors
Gaudet, R.,Wiley, D.C. (deposition date: 2001-07-03, release date: 2001-09-12, Last modification date: 2023-08-16)
Primary citationGaudet, 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: 11532960
DOI: 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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数据于2024-10-30公开中

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