2KYT

Solution structure of the H-REV107 N-terminal domain

Summary for 2KYT

• Entry DOI: 10.2210/pdb2kyt/pdb
• Descriptor: Group XVI phospholipase A2 (1 entity in total)
• Functional Keywords: h-rev107, tumor suppressor, phospholipase, n-terminal domain, hydrolase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P53816
• Total number of polymer chains: 1
• Total formula weight: 13966.92

Authors

Ren, X.,Xia, B. (deposition date: 2010-06-08, release date: 2010-11-03, Last modification date: 2024-05-01)

Primary citation

Ren, X.,Lin, J.,Jin, C.,Xia, B.
Solution structure of the N-terminal catalytic domain of human H-REV107--a novel circular permutated NlpC/P60 domain
Febs Lett., 584:4222-4226, 2010

PubMed Abstract: 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.

PubMed: 20837014
DOI: 10.1016/j.febslet.2010.09.015

Experimental method

SOLUTION NMR