The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Crystal structure of LpxC, a zinc-dependent deacetylase essential for endotoxin biosynthesis
Open accessAbstract
The outer leaflet of the outer membrane of the Gram-negative bacterium serves as a permeability barrier and is composed of lipopolysaccharide, also known as endotoxin. The membrane anchor of lipopolysaccharide is lipid A, the biosynthesis of which is essential for cell viability. The first committed step in lipid A biosynthesis is catalyzed by UDP-(3- O -( R -3-hydroxymyristoyl))- N -acetylglucosamine deacetylase (LpxC), a zinc-dependent deacetylase. Here we report the crystal structure of LpxC from Aquifex aeolicus , which reveals a new α+β fold reflecting primordial gene duplication and fusion, as well as a new zinc-binding motif. The catalytic zinc ion resides at the base of an active-site cleft and adjacent to a hydrophobic tunnel occupied by a fatty acid. This tunnel accounts for the specificity of LpxC toward substrates and inhibitors bearing appropriately positioned 3- O -fatty acid substituents. Notably, simple inhibitors designed to target interactions in the hydrophobic tunnel bind with micromolar affinity, thereby representing a step toward the structure-based design of a potent, broad-spectrum antibacterial drug.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Protein Structure Comparison by Alignment of Distance Matrices
Holm, L., & Sander, C. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1489 · Cited by 3,984
Pathogenetic Mechanisms of Septic Shock
Epstein, F. H., & Parrillo, J. E. (1993) · New England Journal of Medicine · doi:10.1056/nejm199305203282008 · Cited by 1,548
Receptor-Dependent Mechanisms of Cell Stimulation by Bacterial Endotoxin
Ulevitch, R. J., & Tobias, P. S. (1995) · Annual Review of Immunology · doi:10.1146/annurev.iy.13.040195.002253 · Cited by 1,442
Christianson, D. W., & Lipscomb, W. N. (1989) · Accounts of Chemical Research · doi:10.1021/ar00158a003 · Cited by 606
Self-citationStructure of a unique binuclear manganese cluster in arginase
Kanyo, Z. F., Scolnick, L. R., Ash, D. E., & Christianson, D. W. (1996) · Nature · doi:10.1038/383554a0 · Cited by 441
Self-citationBacterial endotoxins: extraordinary lipids that activate eucaryotic signal transduction
Raetz, C. R. (1993) · Journal of Bacteriology · doi:10.1128/jb.175.18.5745-5753.1993 · Cited by 251
Cited by
Recent structural insights into the expanding world of carbohydrate-active enzymes
Davies, G. J., Gloster, T. M., & Henrissat, B. (2005) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2005.10.008 · Cited by 314
Blair, D. E., Schüttelkopf, A. W., MacRae, J. I., & van Aalten, D. M. F. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0504339102 · Cited by 230
Strategies To Design Selective Histone Deacetylase Inhibitors
Melesina, J., Simoben, C. V., Praetorius, L., Bülbül, E. F., Robaa, D., & Sippl, W. (2021) · ChemMedChem · doi:10.1002/cmdc.202000934 · Cited by 118
Structure and reactivity of LpxD, the N -acyltransferase of lipid A biosynthesis
Buetow, L., Smith, T. K., Dawson, A., Fyffe, S., & Hunter, W. N. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0606356104 · Cited by 78
Lonergan, Z. R., Nairn, B. L., Wang, J., Hsu, Y.-P., Hesse, L. E., Beavers, W. N., Chazin, W. J., Trinidad, J. C., VanNieuwenhze, M. S., Giedroc, D. P., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.01.089 · Cited by 76
Metadata
- Authors
- Whittington, D. A., Rusche, K. M., Shin, H., Fierke, C. A., & Christianson, D. W.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2003-06-20
- Volume
- 100
- Issue
- 14
- Pages
- 8146-8150
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2017800476
- Cited by
- 167
- References
- 6
- FWCI
- 7.42
- Type
- journal article
- Language
- en
- Open access
- green
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Crystal structure of LpxC, a zinc-dependent deacetylase essential for endotoxin biosynthesis. https://app.cochat.ai/papers/10.1073/pnas.1432990100
- The paper
- Whittington, D. A., Rusche, K. M., Shin, H., Fierke, C. A., & Christianson, D. W. (2003). Crystal structure of LpxC, a zinc-dependent deacetylase essential for endotoxin biosynthesis. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.1432990100
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
