Cloned (Comment) | Organism |
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- |
Escherichia coli |
Crystallization (Comment) | Organism |
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in complex with inhibotrs acetyl-L-Ile-L-Ala-L-Thr-L-Ala-chloromethylketone, acetyl-L-Phe-L-Ala-L-Thr-L-Ala-chloromethylketone. Inhibitors bind in a substrate-like manner. The S1 subsite is prominent and merges into the water retention site, suggesting intimate interplay between substrate binding, specificity and catalysis. The S4 subsite is plastically formed by residues of the L1 loop, an important but hitherto enigmatic feature of the rhomboid fold | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
acetyl-L-Ile-L-Ala-L-Thr-L-Ala-chloromethylketone | inhibitor derived from the natural rhomboid substrate TatA from bacterium Providencia stuartii, binds in a substrate-like manner | Escherichia coli | |
acetyl-L-Phe-L-Ala-L-Thr-L-Ala-chloromethylketone | inhibitor derived from the natural rhomboid substrate TatA from bacterium Providencia stuartii, binds in a substrate-like manner | Escherichia coli |
Organism | UniProt | Comment | Textmining |
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Escherichia coli | - |
- |
- |