Solution structure of the N-terminal catalytic domain of human H-REV107--a novel circular permutated NlpC/P60 domain.
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.
Ren
Xiaobai
X
Beijing Nuclear Magnetic Resonance Center, Peking University, Beijing, China.
Lin
Jian
J
Jin
Changwen
C
Xia
Bin
B
D000595:Amino Acid Sequence; D017124:Conserved Sequence; D006801:Humans; D047908:Intracellular Signaling Peptides and Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D054512:Phospholipases A2, Calcium-Independent; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D025521:Tumor Suppressor Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
D047908:Intracellular Signaling Peptides and Proteins; D011994:Recombinant Proteins; D025521:Tumor Suppressor Proteins; C490065:PLAAT3 protein, human; D054512:Phospholipases A2, Calcium-Independent