The accessory domain changes the accessibility and molecular topography of the catalytic interface in monomeric GH39 Β-xylosidases

Acta Crystallographica Section D: Biological Crystallography

Volumn 68, Issue 10, 2012, Pages 1339-1345

  Ramos Santos, Camila ^a   Polo, Carla Cristina ^a   Corra, Juliana Moço ^b   Simão, Rita De Cássia Garcia ^b   Seixas, Flavio Augusto Vicente ^c   Murakami, Mario Tyago ^a  

^a BRAZILIAN CENTER FOR RESEARCH IN ENERGY AND MATERIALS CNPEM   (Brazil)

^b UNIVERSIDADE ESTADUAL DO OESTE DO PARANÁ   (Brazil)

^c STATE UNIVERSITY OF MARINGÁ   (Brazil)

Author keywords

Caulobacter crescentus; GH39 xylosidases; oligomerization

Indexed keywords

EXO 1,4 BETA D XYLOSIDASE; EXO-1,4-BETA-D-XYLOSIDASE; XYLAN 1,4 BETA XYLOSIDASE;

ARTICLE; CAULOBACTER CRESCENTUS; CHEMISTRY; ENZYME ACTIVE SITE; ENZYMOLOGY; MOLECULAR DYNAMICS; PROTEIN ANALYSIS; PROTEIN MOTIF; PROTEIN SECONDARY STRUCTURE; SMALL ANGLE SCATTERING; X RAY CRYSTALLOGRAPHY; X RAY DIFFRACTION;

AMINO ACID MOTIFS; CATALYTIC DOMAIN; CAULOBACTER CRESCENTUS; CRYSTALLOGRAPHY, X-RAY; MOLECULAR DYNAMICS SIMULATION; PROTEIN INTERACTION MAPPING; PROTEIN STRUCTURE, SECONDARY; SCATTERING, SMALL ANGLE; X-RAY DIFFRACTION; XYLOSIDASES;

CAULOBACTER VIBRIOIDES;

EID: 84866668560     PISSN: 09074449     EISSN: 13990047     Source Type: Journal    
DOI: 10.1107/S0907444912028491     Document Type: Article

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