1c7o
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(New page: 200px<br /><applet load="1c7o" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c7o, resolution 2.50Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 23:05, 24 November 2007
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CRYSTAL STRUCTURE OF CYSTALYSIN FROM TREPONEMA DENTICOLA CONTAINS A PYRIDOXAL 5'-PHOSPHATE-L-AMINOETHOXYVINYLGLYCINE COMPLEX
Overview
Cystalysin is a C(beta)-S(gamma) lyase from the oral pathogen Treponema, denticola catabolyzing L-cysteine to produce pyruvate, ammonia and H(2)S., With its ability to induce cell lysis, cystalysin represents a new class, of pyridoxal 5'-phosphate (PLP)-dependent virulence factors. The crystal, structure of cystalysin was solved at 1.9 A resolution and revealed a, folding and quaternary arrangement similar to aminotransferases. Based on, the active site architecture, a detailed catalytic mechanism is proposed, for the catabolism of S-containing amino acid substrates yielding H(2)S, and cysteine persulfide. Since no homologies were observed with known, haemolysins the cytotoxicity of cystalysin is attributed to this chemical, reaction. Analysis of the cystalysin-L-aminoethoxyvinylglycine (AVG), complex revealed a 'dead end' ketimine PLP derivative, resulting in a, total loss of enzyme activity. Cystalysin represents an essential factor, of adult periodontitis, therefore the structure of the cystalysin-AVG, complex may provide the chemical basis for rational drug design.
About this Structure
1C7O is a Single protein structure of sequence from Treponema denticola with PPG as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of cystalysin from Treponema denticola: a pyridoxal 5'-phosphate-dependent protein acting as a haemolytic enzyme., Krupka HI, Huber R, Holt SC, Clausen T, EMBO J. 2000 Jul 3;19(13):3168-78. PMID:10880431
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