Abstract
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.
Original language | English (US) |
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Pages (from-to) | 1287-1296 |
Number of pages | 10 |
Journal | Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
Volume | 66 |
Issue number | 10 |
DOIs | |
State | Published - Oct 2010 |
Externally published | Yes |
Keywords
- gut microbiome
- immunoglobulin-like fold
- jelly-roll fold
- structural genomics
- sugars
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Genetics
- Condensed Matter Physics