6lcf

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Crystal Structure of beta-L-arabinobiose binding protein - nativeCrystal Structure of beta-L-arabinobiose binding protein - native

Structural highlights

6lcf is a 2 chain structure with sequence from As 1.2186. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:APC1462_0182, APC1476_0195, APC1503_0213, APS65_00860, BBG7_0210, BL105A_0201, DPC6316_0214, DPC6317_0191, DW237_03380, DW792_04665, DWV59_05050, DWV93_04885, DWZ73_01175, EAI75_02995, HMPREF0177_01141 (AS 1.2186)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

Bifidobacterium longum is a symbiotic human gut bacterium that has a degradation system for beta-arabinooligosaccharides, which are present in the hydroxyproline-rich glycoproteins of edible plants. Whereas microbial degradation systems for alpha-linked arabinofuranosyl carbohydrates have been extensively studied, little is understood about the degradation systems targeting beta-linked arabinofuranosyl carbohydrates. We functionally and structurally analyzed a substrate-binding protein (SBP) of a putative ABC transporter (BLLJ_0208) in the beta-arabinooligosaccharide degradation system. Thermal shift assays and isothermal titration calorimetry revealed that the SBP specifically bound Araf-beta1,2-Araf (beta-Ara2 ) with a Kd of 0.150 mum, but did not bind L-arabinose or methyl-beta-Ara2 . Therefore, the SBP was termed beta-arabinobiose-binding protein (BABP). Crystal structures of BABP complexed with beta-Ara2 were determined at resolutions of up to 1.78 A. The findings showed that beta-Ara2 was bound to BABP within a short tunnel between two lobes as an alpha-anomeric form at its reducing end. BABP forms extensive interactions with beta-Ara2 , and its binding mode was unique among SBPs. A molecular dynamics simulation revealed that the closed conformation of substrate-bound BABP is stable, whereas substrate-free form can adopt a fully open and two distinct semi-open states. The importer system specific for beta-Ara2 may contribute to microbial survival in biological niches with limited amounts of digestible carbohydrates. DATABASE: Atomic coordinates and structure factors (codes 6LCE and 6LCF) have been deposited in the Protein Data Bank (http://wwpdb.org/).

Structural analysis of beta-L-arabinobiose-binding protein in the metabolic pathway of hydroxyproline-rich glycoproteins in Bifidobacterium longum.,Miyake M, Terada T, Shimokawa M, Sugimoto N, Arakawa T, Shimizu K, Igarashi K, Fujita K, Fushinobu S FEBS J. 2020 Apr 4. doi: 10.1111/febs.15315. PMID:32246585[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Miyake M, Terada T, Shimokawa M, Sugimoto N, Arakawa T, Shimizu K, Igarashi K, Fujita K, Fushinobu S. Structural analysis of beta-L-arabinobiose-binding protein in the metabolic pathway of hydroxyproline-rich glycoproteins in Bifidobacterium longum. FEBS J. 2020 Apr 4. doi: 10.1111/febs.15315. PMID:32246585 doi:http://dx.doi.org/10.1111/febs.15315

6lcf, resolution 1.92Å

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