Open AccessStructure of BT_3984, a member of the SusD/RagB family of nutrient‐binding molecules
Author(s) -
Bakolitsa Constantina,
Xu Qingping,
Rife Christopher L.,
Abdubek Polat,
Astakhova Tamara,
Axelrod Herbert L.,
Carlton Dennis,
Chen Connie,
Chiu HsiuJu,
Clayton Thomas,
Das Debanu,
Deller Marc C.,
Duan Lian,
Ellrott Kyle,
Farr Carol L.,
Feuerhelm Julie,
Grant Joanna C.,
Grzechnik Anna,
Han Gye Won,
Jaroszewski Lukasz,
Jin Kevin K.,
Klock Heath E.,
Knuth Mark W.,
Kozbial Piotr,
Krishna S. Sri,
Kumar Abhinav,
Lam Winnie W.,
Marciano David,
McMullan Daniel,
Miller Mitchell D.,
Morse Andrew T.,
Nigoghossian Edward,
Nopakun Amanda,
Okach Linda,
Puckett Christina,
Reyes Ron,
Tien Henry J.,
Trame Christine B.,
Van Den Bedem Henry,
Weekes Dana,
Hodgson Keith O.,
Wooley John,
Elsliger MarcAndré,
Deacon Ashley M.,
Godzik Adam,
Lesley Scott A.,
Wilson Ian A.
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110032999
Subject(s) - bacteroides thetaiotaomicron , tetratricopeptide , operon , glycan , biology , chemistry , computational biology , microbiology and biotechnology , biochemistry , genetics , gene , bacteroides , glycoprotein , bacteria , escherichia coli
The crystal structure of the Bacteroides thetaiotaomicron protein BT_3984 was determined to a resolution of 1.7 Å and was the first structure to be determined from the extensive SusD family of polysaccharide‐binding proteins. SusD is an essential component of the sus operon that defines the paradigm for glycan utilization in dominant members of the human gut microbiota. Structural analysis of BT_3984 revealed an N‐terminal region containing several tetratricopeptide repeats (TPRs), while the signature C‐terminal region is less structured and contains extensive loop regions. Sequence and structure analysis of BT_3984 suggests the presence of binding interfaces for other proteins from the polysaccharide‐utilization complex.