Crystal structures of a family 8 polysaccharide lyase reveal open and highly occluded substrate-binding cleft conformations
about
Induced-fit motion of a lid loop involved in catalysis in alginate lyase A1-IIIInsight into the role of substrate-binding residues in conferring substrate specificity for the multifunctional polysaccharide lyase Smlt1473.Chondroitin Lyase from a Marine Arthrobacter sp. MAT3885 for the Production of Chondroitin Sulfate Disaccharides.Reptation-induced coalescence of tunnels and cavities in Escherichia Coli XylE transporter conformers accounts for facilitated diffusion.The crystal structure of novel chondroitin lyase ODV-E66, a baculovirus envelope protein.Functional role of R462 in the degradation of hyaluronan catalyzed by hyaluronate lyase from Streptococcus pneumoniae.
P2860
Crystal structures of a family 8 polysaccharide lyase reveal open and highly occluded substrate-binding cleft conformations
description
2011 nî lūn-bûn
@nan
2011 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի մարտին հրատարակված գիտական հոդված
@hy
2011年の論文
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2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Crystal structures of a family ...... te-binding cleft conformations
@ast
Crystal structures of a family ...... te-binding cleft conformations
@en
Crystal structures of a family ...... te-binding cleft conformations
@nl
type
label
Crystal structures of a family ...... te-binding cleft conformations
@ast
Crystal structures of a family ...... te-binding cleft conformations
@en
Crystal structures of a family ...... te-binding cleft conformations
@nl
prefLabel
Crystal structures of a family ...... te-binding cleft conformations
@ast
Crystal structures of a family ...... te-binding cleft conformations
@en
Crystal structures of a family ...... te-binding cleft conformations
@nl
P2093
P2860
P50
P356
P1433
P1476
Crystal structures of a family ...... te-binding cleft conformations
@en
P2093
Meng Zhang
Nicola L Smith
Simon J Charnock
Zainab H Elmabrouk
P2860
P304
P356
10.1002/PROT.22938
P407
P577
2011-03-01T00:00:00Z