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PROSITE documentation PDOC51995 |
The ~200-residue anthrax toxin lethal factor (ATLF)-like domain is found in one or two copies in the following proteins:
The ATLF-like domain acts either as a metalloprotease domain, forming the M34 family of metalloendopeptidases, (ATLF domain IV, PPEP-1 and 2) or as an anthrax protective antigen-binding domain (PABD) (ATLF domain I and EF and Certhrax PABD).
The ATLF-like domain is composed of a four-stranded β-sheet and a helical bundle backing the β-sheet (see <PDB:A0P>). All catalytically active ATLF-like domains exhibit the conserved sequence motif HEXXH, where the two histidines ligate the catalytic zinc ion, and the glutamic acid acts as catalytic base activating a zinc-bound water molecule for nucleophilic attack on the scissile peptide bond [1,2,3,5,6].
The profile we developed covers the entire ATLF-like domain.
Last update:March 2022 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
1 | Authors | Pannifer A.D. Wong T.Y. Schwarzenbacher R. Renatus M. Petosa C. Bienkowska J. Lacy D.B. Collier R.J. Park S. Leppla S.H. Hanna P. Liddington R.C. |
Title | Crystal structure of the anthrax lethal factor. | |
Source | Nature 414:229-233(2001). | |
PubMed ID | 11700563 | |
DOI | 10.1038/n35101998 |
2 | Authors | Shen Y. Zhukovskaya N.L. Guo Q. Florian J. Tang W.-J. |
Title | Calcium-independent calmodulin binding and two-metal-ion catalytic mechanism of anthrax edema factor. | |
Source | EMBO. J. 24:929-941(2005). | |
PubMed ID | 15719022 | |
DOI | 10.1038/sj.emboj.7600574 |
3 | Authors | Visschedyk D. Rochon A. Tempel W. Dimov S. Park H.-W. Merrill A.R. |
Title | Certhrax toxin, an anthrax-related ADP-ribosyltransferase from Bacillus cereus. | |
Source | J. Biol. Chem. 287:41089-41102(2012). | |
PubMed ID | 22992735 | |
DOI | 10.1074/jbc.M112.412809 |
4 | Authors | Hensbergen P.J. Klychnikov O.I. Bakker D. van Winden V.J.C. Ras N. Kemp A.C. Cordfunke R.A. Dragan I. Deelder A.M. Kuijper E.J. Corver J. Drijfhout J.W. van Leeuwen H.C. |
Title | A novel secreted metalloprotease (CD2830) from Clostridium difficile cleaves specific proline sequences in LPXTG cell surface proteins. | |
Source | Mol. Cell. Proteomics. 13:1231-1244(2014). | |
PubMed ID | 24623589 | |
DOI | 10.1074/mcp.M113.034728 |
5 | Authors | Schacherl M. Pichlo C. Neundorf I. Baumann U. |
Title | Structural Basis of Proline-Proline Peptide Bond Specificity of the Metalloprotease Zmp1 Implicated in Motility of Clostridium difficile. | |
Source | Structure 23:1632-1642(2015). | |
PubMed ID | 26211609 | |
DOI | 10.1016/j.str.2015.06.018 |
6 | Authors | Klychnikov O.I. Shamorkina T.M. Weeks S.D. van Leeuwen H.C. Corver J. Drijfhout J.W. van Veelen P.A. Sluchanko N.N. Strelkov S.V. Hensbergen P.J. |
Title | Discovery of a new Pro-Pro endopeptidase, PPEP-2, provides mechanistic insights into the differences in substrate specificity within the PPEP family. | |
Source | J. Biol. Chem. 293:11154-11165(2018). | |
PubMed ID | 29794027 | |
DOI | 10.1074/jbc.RA118.003244 |