3dgt

From Proteopedia

Jump to: navigation, search

The 1.5 A crystal structure of endo-1,3-beta-glucanase from Streptomyces sioyaensis

Structural highlights

3dgt is a 1 chain structure with sequence from Atcc 13989. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:MG
Activity:Glucan endo-1,3-beta-D-glucosidase, with EC number 3.2.1.39
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The catalytic domain structure of Streptomyces sioyaensis 1,3-beta-glucanase (278 amino acids), a member of glycosyl hydrolase family 16 (GHF16), was determined to 1.5 A resolution in space group P2(1)2(1)2(1). The enzyme specifically hydrolyzes the glycosidic bond of the 1,3-beta-linked glucan substrate. The overall structure contains two antiparallel six-and seven-stranded beta-sheets stacked in a beta-sandwich jelly-roll motif similar to the fold of GHF16 1,3-1,4-beta-glucanases. The active-site cleft of the enzyme is distinct, with the closure of one end primarily caused by two protruding loop insertions and two key residues, Tyr38 and Tyr134. The current known structures of 1,3-1,4-beta-glucanases and 1,3-beta-glucanase from Nocardiopsis sp., on the other hand, have open-channel active-site clefts that can accommodate six beta-D-glucopyranosyl units. The active-site structure of 1,3-beta-glucanase was compared with those of other homologous structures in order to address the binding and enzymatic specificity for 1,3-beta-linked glucans in Streptomyces. This information could be helpful in the development of specific antifungal agents.

The 1.5 A structure of endo-1,3-beta-glucanase from Streptomyces sioyaensis: evolution of the active-site structure for 1,3-beta-glucan-binding specificity and hydrolysis.,Hong TY, Hsiao YY, Meng M, Li TT Acta Crystallogr D Biol Crystallogr. 2008 Sep;64(Pt 9):964-70. Epub 2008, Aug 13. PMID:18703845[1]

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

Loading citation details..
Citations
reviews cite this structure
No citations found

See Also

References

  1. Hong TY, Hsiao YY, Meng M, Li TT. The 1.5 A structure of endo-1,3-beta-glucanase from Streptomyces sioyaensis: evolution of the active-site structure for 1,3-beta-glucan-binding specificity and hydrolysis. Acta Crystallogr D Biol Crystallogr. 2008 Sep;64(Pt 9):964-70. Epub 2008, Aug 13. PMID:18703845 doi:10.1107/S0907444908021550

Contents


PDB ID 3dgt

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools