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Solution structure of the N‐terminal catalytic domain of human H‐REV107 – A novel circular permutated NlpC/P60 domain
Author(s) -
Ren Xiaobai,
Lin Jian,
Jin Changwen,
Xia Bin
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2010.09.015
Subject(s) - catalytic triad , active site , biochemistry , phospholipase , enzyme , biology , chemistry , protein domain , protein structure , acyltransferase , gene
H‐REV107 is a Ca 2+ ‐independent phospholipase A 1/2 , and it is also a pro‐apoptosis protein belonging to the novel class II tumor suppressor family, H‐REV107‐like family. Here we report the solution structure of the N‐terminal catalytic domain of human H‐REV107, which has a similar architecture to classical NlpC/P60 domains, even though their fold topologies are different due to circular permutation in the primary sequence. The phospholipase active site possesses a structurally conserved Cys–His–His catalytic triad as found in NlpC/P60 peptidases, indicating H‐REV107 should adopt a similar catalytic mechanism towards phospholipid substrates to that of NlpC/P60 peptidases towards peptides. As H‐REV107 is highly similar to lecithin retinol acyltransferase, our study also provides structural insight to this essential enzyme in retinol metabolism.