Literature DB >> 29574769

Crystal structure of exo-rhamnogalacturonan lyase from Penicillium chrysogenum as a member of polysaccharide lyase family 26.

Yuika Kunishige1, Marin Iwai1, Masami Nakazawa1, Mitsuhiro Ueda1, Toshiji Tada2, Shigenori Nishimura1, Tatsuji Sakamoto1.   

Abstract

Exo-rhamnogalacturonan lyase from Penicillium chrysogenum 31B (PcRGLX) was recently classified as a member of polysaccharide lyase (PL) family 26 along with hypothetical proteins derived from various organisms. In this study, we determined the crystal structure of PcRGLX as the first structure of a member of this family. Based on the substrate-binding orientation and substrate specificity, PcRGLX is an exo-type PL that cleaves rhamnogalacturonan from the reducing end. Analysis of PcRGLX-complex structures with reaction products indicate that the active site possesses an L-shaped cleft that can accommodate galactosyl side chains, suggesting side-chain-bypassing activity in PcRGLX. Furthermore, we determined the residues critical for catalysis by analyzing the enzyme activities of inactive variants.
© 2018 Federation of European Biochemical Societies.

Entities:  

Keywords:  crystal structure; exo-rhamnogalacturonan lyase; polysaccharide lyase family 26

Mesh:

Substances:

Year:  2018        PMID: 29574769     DOI: 10.1002/1873-3468.13034

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  3 in total

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  3 in total

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