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6SHD

Structure of the GH76A alpha-1,6-mannanase from Salegentibacter sp. HEL1_6

Summary for 6SHD
Entry DOI10.2210/pdb6shd/pdb
DescriptorAlpha-1,6-mannanase (2 entities in total)
Functional Keywordsmannanase, glycoside hydrolase, gh76, cazyme, mannan, carbohydrate, hydrolase
Biological sourceSalegentibacter sp. Hel_I_6
Total number of polymer chains3
Total formula weight131242.54
Authors
Hehemann, J.H.,Solanki, V. (deposition date: 2019-08-06, release date: 2020-08-26, Last modification date: 2024-01-24)
Primary citationSolanki, V.,Kruger, K.,Crawford, C.J.,Pardo-Vargas, A.,Danglad-Flores, J.,Hoang, K.L.M.,Klassen, L.,Abbott, D.W.,Seeberger, P.H.,Amann, R.I.,Teeling, H.,Hehemann, J.H.
Glycoside hydrolase from the GH76 family indicates that marine Salegentibacter sp. Hel_I_6 consumes alpha-mannan from fungi.
Isme J, 2022
Cited by
PubMed Abstract: Microbial glycan degradation is essential to global carbon cycling. The marine bacterium Salegentibacter sp. Hel_I_6 (Bacteroidota) isolated from seawater off Helgoland island (North Sea) contains an α-mannan inducible gene cluster with a GH76 family endo-α-1,6-mannanase (ShGH76). This cluster is related to genetic loci employed by human gut bacteria to digest fungal α-mannan. Metagenomes from the Hel_I_6 isolation site revealed increasing GH76 gene frequencies in free-living bacteria during microalgae blooms, suggesting degradation of α-1,6-mannans from fungi. Recombinant ShGH76 protein activity assays with yeast α-mannan and synthetic oligomannans showed endo-α-1,6-mannanase activity. Resolved structures of apo-ShGH76 (2.0 Å) and of mutants co-crystalized with fungal mannan-mimicking α-1,6-mannotetrose (1.90 Å) and α-1,6-mannotriose (1.47 Å) retained the canonical (α/α) fold, despite low identities with sequences of known GH76 structures (GH76s from gut bacteria: <27%). The apo-form active site differed from those known from gut bacteria, and co-crystallizations revealed a kinked oligomannan conformation. Co-crystallizations also revealed precise molecular-scale interactions of ShGH76 with fungal mannan-mimicking oligomannans, indicating adaptation to this particular type of substrate. Our data hence suggest presence of yet unknown fungal α-1,6-mannans in marine ecosystems, in particular during microalgal blooms.
PubMed: 35414716
DOI: 10.1038/s41396-022-01223-w
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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