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This family contains a number of integral outer membrane serine proteases that differ from trypsin-like proteases in that they cleave polypeptides between two basically charged amino acids. Escherichia coli OmpT protein has previously been classified as a serine protease with Ser(99) and His(212) as active site residues. The X-ray structure of the Enzyme is inconsistent with this classification, and the involvement of a nucleophilic water molecule, activated by the residue pair Asp(210)/His(212), classifies the enzyme as an aspartic endopeptidase with the activity also strongly dependent on Asp(83) and Asp(85). Both may function in binding of the water molecule and/or in oxyanion stabilization. The transmembrane ß-barrel, consists of 10 beta-strands, and the enzymatic activity depends on reversible dimerization.
Omptin proteins: an expanding family of outer membrane proteases in Gram-negative Enterobacteriaceae
Mol Membr Biol. 2007 Sep-Dec;24(5-6):395-406. doi: 10.1080/09687680701443822.
Identification of essential acidic residues of outer membrane protease OmpT supports a novel active site
FEBS Lett. 2001 Sep 21;505(3):426-30. doi: 10.1016/s0014-5793(01)02863-0.
The omptin family of enterobacterial surface proteases/adhesins: from housekeeping in Escherichia coli to systemic spread of Yersinia pestis
Int J Med Microbiol. 2004 Jul;294(1):7-14. doi: 10.1016/j.ijmm.2004.01.003.
Substrate specificity of the Escherichia coli outer membrane protease OmpT
J Bacteriol. 2004 Sep;186(17):5919-25. doi: 10.1128/JB.186.17.5919-5925.2004.
Structural biology of membrane-intrinsic beta-barrel enzymes: sentinels of the bacterial outer membrane
Biochim Biophys Acta. 2008 Sep;1778(9):1881-96. doi: 10.1016/j.bbamem.2007.07.021. Epub 2007 Aug 11.
Crystal structure of the outer membrane protease OmpT from Escherichia coli suggests a novel catalytic site
EMBO J. 2001 Sep 17;20(18):5033-9. doi: 10.1093/emboj/20.18.5033.
An active site water network in the plasminogen activator pla from Yersinia pestis
Structure. 2010 Jul 14;18(7):809-18. doi: 10.1016/j.str.2010.03.013.
|Proteins in this family with 3D-structure|