3nqz
Crystal structure of the autoprocessed Vibriolysin MCP-02 with E369A mutationCrystal structure of the autoprocessed Vibriolysin MCP-02 with E369A mutation
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThermolysin-like proteases (TLPs), a large group of zinc metalloproteases, are synthesized as inactive precursors. TLPs with a long propeptide ( approximately 200 residues) undergo maturation following autoprocessing through an elusive molecular mechanism. We report the first two crystal structures for the autoprocessed complexes of a typical TLP, MCP-02. In the autoprocessed complex, Ala205 shifts upward by 33 A from the previously covalently linked residue, His204, indicating that, following autocleavage of the peptide bond between His204 and Ala205, a large conformational change from the zymogen to the autoprocessed complex occurs. The eight N-terminal residues (residues Ala205-Gly212) of the catalytic domain form a new beta-strand, nestling into two other beta-strands. Simultaneously, the apparent T(m) of the autoprocessed complex increases 20 degrees C compared to that of the zymogen. The stepwise degradation of the propeptide begins with two sequential cuttings at Ser49-Val50 and Gly57-Leu58, which lead to the disassembly of the propeptide and the formation of mature MCP-02. Our findings give new insights into the molecular mechanism of TLP maturation. Structural basis for the autoprocessing of zinc metalloproteases in the thermolysin family.,Gao X, Wang J, Yu DQ, Bian F, Xie BB, Chen XL, Zhou BC, Lai LH, Wang ZX, Wu JW, Zhang YZ Proc Natl Acad Sci U S A. 2010 Oct 12;107(41):17569-74. Epub 2010 Sep 27. PMID:20876133[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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