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Insight into the structure of an endopolygalacturonase from the phytopathogen Burkholderia cepacia: A biochemical and computational study
Authors:Claudia Massa  Corrado Guarnaccia  Doriano Lamba  Claudio Anselmi
Affiliation:1. Structural Biology Laboratory, Sincrotrone Trieste S.C.p.A., AREA Science Park – Basovizza Strada Statale 14, km 163,5, I-34149 Trieste, Italy;2. ICGEB, International Centre for Genetic Engineering and Biotechnology, Area Science Park Padriciano 99, I-34012 Trieste, Italy;3. Istituto di Cristallografia-C.N.R., Unità Organizzativa di Supporto, Sede di Trieste Area Science Park-Basovizza Strada Statale 14, km 163,5, I-34149 Trieste, Italy;4. ISAS, International School for Advanced Studies, Statistical and Biological Physics, Via Beirut 2/4, I-34014 Trieste, Italy
Abstract:We have recently investigated and characterized the mode of action of BcPeh28A, an endopolygalacturonase (endoPG) from the phytopathogen Burkholderia cepacia. EndoPGs belong to glycoside hydrolase family 28 and are responsible for the hydrolysis of the non-esterified regions of pectins.
Keywords:Disulphide bridges mapping   MALDI mass spectrometry   Fold recognition   Low homology   Molecular dynamics
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