Open AccessStructure of Bacteroides thetaiotaomicron BT2081 at 2.05 Å resolution: the first structural representative of a new protein family that may play a role in carbohydrate metabolism
Author(s) -
Yeh Andrew P.,
Abdubek Polat,
Astakhova Tamara,
Axelrod Herbert L.,
Bakolitsa Constantina,
Cai Xiaohui,
Carlton Dennis,
Chen Connie,
Chiu HsiuJu,
Chiu Michelle,
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,
Wooten Tiffany,
Xu Qingping,
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/s1744309110028228
Subject(s) - bacteroides thetaiotaomicron , biochemistry , bacteroides , glycoside hydrolase , context (archaeology) , carbohydrate , chemistry , biology , bacteroidetes , crystallography , genetics , bacteria , enzyme , gene , paleontology , 16s ribosomal rna
BT2081 from Bacteroides thetaiotaomicron (GenBank accession code NP_810994.1) is a member of a novel protein family consisting of over 160 members, most of which are found in the different classes of Bacteroidetes. Genome‐context analysis lends support to the involvement of this family in carbohydrate metabolism, which plays a key role in B. thetaiotaomicron as a predominant bacterial symbiont in the human distal gut microbiome. The crystal structure of BT2081 at 2.05 Å resolution represents the first structure from this new protein family. BT2081 consists of an N‐terminal domain, which adopts a β‐sandwich immunoglobulin‐like fold, and a larger C‐terminal domain with a β‐sandwich jelly‐roll fold. Structural analyses reveal that both domains are similar to those found in various carbohydrate‐active enzymes. The C‐terminal β‐jelly‐roll domain contains a potential carbohydrate‐binding site that is highly conserved among BT2081 homologs and is situated in the same location as the carbohydrate‐binding sites that are found in structurally similar glycoside hydrolases (GHs). However, in BT2081 this site is partially occluded by surrounding loops, which results in a deep solvent‐accessible pocket rather than a shallower solvent‐exposed cleft.