| Literature DB >> 29574769 |
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.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