Solution structure of the N‐terminal catalytic domain of human H‐REV107 – A novel circular permutated NlpC/P60 domain
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.
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In HRASLS3, the catalytic Cys residue is fully accessible to the solvent because of the reduced size of the loop between β-strands 3 and 4 and its flexible conformations as shown by NMR data.
“Because of the reduced size of the loop between β-strands 3 and 4 and its flexible conformations as shown by NMR data [114], the catalytic Cys residue in HRASLS3 is fully accessible to the solvent.”
From Molecular Basis for Vitamin A Uptake and Storage in Vertebrates (2016) · cites this paper as [114]
Cites
Anantharaman, V., & Aravind, L. (2003) · Genome Biology · doi:10.1186/gb-2003-4-2-r11 · Cited by 365 · see citing works
Topology and Membrane Association of Lecithin: Retinol Acyltransferase
Moise, A. R., Golczak, M., Imanishi, Y., & Palczewski, K. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m608315200 · Cited by 59 · cited 11× · see citing works
“The structure of HREV107N is also the first structure of LRAT family, which may provide structural insight for understanding the mechanism of LRAT.”
BackgroundInfluentialRoles of Cysteine 161 and Tyrosine 154 in the Lecithin−Retinol Acyltransferase Mechanism
Xue, L., & Rando, R. R. (2004) · Biochemistry · doi:10.1021/bi049556f · Cited by 28 · see citing works
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Structural Basis for the Acyltransferase Activity of Lecithin:Retinol Acyltransferase-like Proteins
Golczak, M., Kiser, P. D., Sears, A. E., Lodowski, D. T., Blaner, W. S., & Palczewski, K. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.361550 · Cited by 77 · see citing works
Molecular Basis for Vitamin A Uptake and Storage in Vertebrates
Chelstowska, S., Widjaja-Adhi, M., Silvaroli, J., & Golczak, M. (2016) · Nutrients · doi:10.3390/nu8110676 · Cited by 69 · see citing works
“Because of the reduced size of the loop between β‐strands 3 and 4 and its flexible conformations as shown by NMR data [114], the catalytic Cys residue in HRASLS3 is fully accessible to the solvent.”
BackgroundLrat-specific domain facilitates Vitamin A metabolism by domain swapping in HRASLS3
Golczak, M., Sears, A. E., Kiser, P. D., & Palczewski, K. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1687 · Cited by 58 · see citing works
Bussières, S., Cantin, L., Desbat, B., & Salesse, C. (2012) · Langmuir · doi:10.1021/la203896n · Cited by 20 · see citing works
- Authors
- Ren, X., Lin, J., Jin, C., & Xia, B.
- Affiliations
- Peking University (CN)
- Corresponding author
- Lin, Jian
- Xia, Bin
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2010-09-15
- Volume
- 584
- Issue
- 19
- Pages
- 4222-4226
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2094584063
- Cited by
- 29
- References
- 3
- Citations by year
- 2024: 1 · 2023: 2 · 2022: 2 · 2021: 1 · 2020: 3 · 2019: 2 · 2018: 1 · 2017: 2 · 2016: 1 · 2015: 2 · 2014: 3 · 2013: 2 · 2012: 6
- FWCI
- 1.17
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- FEBS Letters (publishedVersion)
- PubMed (publishedVersion)
- Funders
- 973 Program of China (2009CB521703)
- National Science Foundation of China (30125009, 30800172)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- circular permutation, solution structure, catalytic triad, LRAT, vitamin A metabolism, phospholipid hydrolysis
- MeSH terms
- Amino Acid Sequence, Humans, Models, Molecular, Molecular Sequence Data, Recombinant Proteins, Conserved Sequence, Sequence Homology, Amino Acid, Protein Structure, Tertiary, Protein Folding, Nuclear Magnetic Resonance, Biomolecular, Tumor Suppressor Proteins, Intracellular Signaling Peptides and Proteins, Phospholipases A2, Calcium-Independent
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