Structure-specificity relationships in Abp, a GH27 β-l-arabinopyranosidase from Geobacillus stearothermophilus T6

Acta Crystallographica Section D: Biological Crystallography

Volumn 70, Issue 11, 2014, Pages 2994-3012

  Lansky, Shifra ^a   Salama, Rachel ^b   Solomon, Hodaya V ^a   Feinberg, Hadar ^a   Belrhali, Hassan ^c   Shoham, Yuval ^b   Shoham, Gil ^a  

^a HEBREW UNIVERSITY OF JERUSALEM   (Israel)

^b TECHNION ISRAEL INSTITUTE OF TECHNOLOGY   (Israel)

^c UNIV GRENOBLE ALPES   (France)

Author keywords

arabinan utilization; arabinopyranosidase; arabinose; catalytic mutant; electrostatic potential; Geobacillus stearothermophilus; GH27; glycoside hydrolase; negative electrostatic patch; oligomerization; retaining mechanism; SAXS

Indexed keywords

ARABINOSE; GLYCOSIDASE;

CHEMICAL STRUCTURE; CHEMISTRY; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; ENZYMOLOGY; GENETICS; GEOBACILLUS STEAROTHERMOPHILUS; METABOLISM; POINT MUTATION; PROTEIN CONFORMATION; PROTEIN MULTIMERIZATION; SMALL ANGLE SCATTERING; X RAY CRYSTALLOGRAPHY; X RAY DIFFRACTION;

ARABINOSE; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; GEOBACILLUS STEAROTHERMOPHILUS; GLYCOSIDE HYDROLASES; MODELS, MOLECULAR; POINT MUTATION; PROTEIN CONFORMATION; PROTEIN MULTIMERIZATION; SCATTERING, SMALL ANGLE; SUBSTRATE SPECIFICITY; X-RAY DIFFRACTION;

EID: 84908614736     PISSN: 09074449     EISSN: 13990047     Source Type: Journal    
DOI: 10.1107/S139900471401863X     Document Type: Article

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