Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1F8Q

CRYSTAL STRUCTURE OF ALPHA-MOMORCHARIN IN ACETONITRILE-WATER MIXTURE

Summary for 1F8Q
Entry DOI10.2210/pdb1f8q/pdb
Related1mri
DescriptorALPHA-MOMORCHARIN, alpha-D-xylopyranose-(1-2)-alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, PENTANEDIAL, ... (5 entities in total)
Functional Keywordsribosome-inactivating protein, organic slovent, momorcharin, hydrolase
Biological sourceMomordica charantia (balsam pear)
Total number of polymer chains1
Total formula weight30219.08
Authors
Zhu, G.,Huang, Q.,Qian, M.,Tang, Y. (deposition date: 2000-07-03, release date: 2000-07-26, Last modification date: 2024-11-20)
Primary citationZhu, G.,Huang, Q.,Qian, M.,Tang, Y.
Crystal structure of alpha-momorcharin in 80% acetonitrile--water mixture
BIOCHIM.BIOPHYS.ACTA, 1548:152-158, 2001
Cited by
PubMed Abstract: Crystals of alpha-momorcharin (MMC) were cross-linked and soaked in an 80% acetonitrile--water mixture and X-ray data were collected to 2.2 A resolution. MMC is a ribosome-inactivating protein with a sugar chain on Asn-227. In previous studies, the whole conformation of the sugar chain could not be obtained in the aqueous system. Here the structure of MMC in a low water system is shown to be similar to the native one, but the sugar chain on Asn-227 is defined by the electron density map. Several oxygen atoms of the oligosaccharide formed intramolecular hydrogen bonds to the protein moiety. The conformation of the residues in the active center is similar to that in the aqueous system. Our results show conformational alteration of the tetrasaccharide of MMC in organic media. They indicate that the oligosaccharides are more rigid in organic solvents. X-ray determination in organic media may be used to solve some structures of oligosaccharides linked to glycoproteins.
PubMed: 11451448
DOI: 10.1016/S0167-4838(01)00235-7
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

237735

数据于2025-06-18公开中

PDB statisticsPDBj update infoContact PDBjnumon