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5AON

Crystal structure of the conserved N-terminal domain of Pex14 from Trypanosoma brucei

Summary for 5AON
Entry DOI10.2210/pdb5aon/pdb
DescriptorPEROXIN 14, SULFATE ION (3 entities in total)
Functional Keywordsperoxisomal matrix protein import receptor, signaling protein
Biological sourceTRYPANOSOMA BRUCEI
Total number of polymer chains5
Total formula weight30032.13
Authors
Obita, T.,Sugawara, Y.,Mizuguchi, M.,Watanabe, Y.,Kawaguchi, K.,Imanaka, T. (deposition date: 2015-09-11, release date: 2015-12-23, Last modification date: 2024-01-10)
Primary citationWatanabe, Y.,Kawaguchi, K.,Okuyama, N.,Sugawara, Y.,Obita, T.,Mizuguchi, M.,Morita, M.,Imanaka, T.
Characterization of the Interaction between Trypanosoma Brucei Pex5P and its Receptor Pex14P.
FEBS Lett., 590:242-, 2016
Cited by
PubMed Abstract: The interaction of Trypanosoma brucei (Tb) Pex5p and its receptor TbPex14p is essential for the translocation of newly synthesized matrix proteins into the glycosome. Here, we reveal that only the third WXXXF/Y motif of TbPex5p is involved in the interaction and that negative charge of the fourth amino acid is important. We suggest that Phe35 and Phe52 of TbPex14p interact with Trp318 and Phe322 in the third motif and that the Lys56 adjacent to Phe35/Phe52 associates with the fourth Glu in the motif to make the complex. This information is expected to be useful for developing anti-trypanosomal drugs.
PubMed: 26762183
DOI: 10.1002/1873-3468.12044
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.646 Å)
Structure validation

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数据于2025-06-25公开中

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