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Structure paper

TitleThe X-Ray Crystal Structure of an Arthrobacter Protophormiae Endo-Beta-N-Acetylglucosaminidase Reveals a (Beta/Alpha)(8) Catalytic Domain, Two Ancillary Domains and Active Site Residues Key for Transglycosylation Activity.
Journal, issue, pagesJ. Mol. Biol., Vol. 389, Page 1-, Year 2009
Publish dateMay 14, 2008 (structure data deposition date)
AuthorsSuits, M.D. / Ling, Z. / Bingham, R.J. / Bruce, N.C. / Davies, G.J. / Fairbanks, A.J. / Moir, J.W. / Taylor, E.J.
External linksJ. Mol. Biol. / PubMed:19327363
MethodsX-ray diffraction
Resolution1.79 Å
Structure data

PDB-2vtf:
X-ray crystal structure of the Endo-beta-N-acetylglucosaminidase from Arthrobacter protophormiae E173Q mutant reveals a TIM barrel catalytic domain and two ancillary domains
Method: X-RAY DIFFRACTION / Resolution: 1.79 Å

Chemicals

ChemComp-B3P:
2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH buffer*YM

ChemComp-PGE:
TRIETHYLENE GLYCOL

ChemComp-HOH:
WATER

Source
  • arthrobacter protophormiae (bacteria)
KeywordsHYDROLASE / FAMILY 85 / GLYCOSIDASE / ARTHROBACTER / CARBOHYDRATE BINDING / ACETYLGLUCOSAMINIDASE

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