1cf5

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[[Image:1cf5.gif|left|200px]]
[[Image:1cf5.gif|left|200px]]
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{{Structure
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|PDB= 1cf5 |SIZE=350|CAPTION= <scene name='initialview01'>1cf5</scene>, resolution 2.550&Aring;
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The line below this paragraph, containing "STRUCTURE_1cf5", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=XYP:BETA-D-XYLOPYRANOSE'>XYP</scene>
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{{STRUCTURE_1cf5| PDB=1cf5 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cf5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cf5 OCA], [http://www.ebi.ac.uk/pdbsum/1cf5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cf5 RCSB]</span>
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'''BETA-MOMORCHARIN STRUCTURE AT 2.55 A'''
'''BETA-MOMORCHARIN STRUCTURE AT 2.55 A'''
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[[Category: Xiong, J P.]]
[[Category: Xiong, J P.]]
[[Category: Yuan, Y R.]]
[[Category: Yuan, Y R.]]
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[[Category: glycoprotein]]
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[[Category: Glycoprotein]]
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[[Category: ribosome-inactivating protein]]
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[[Category: Ribosome-inactivating protein]]
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[[Category: rna n-glycosidase activity]]
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[[Category: Rna n-glycosidase activity]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:39:54 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:20:26 2008''
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Revision as of 09:39, 2 May 2008

Image:1cf5.gif

Template:STRUCTURE 1cf5

BETA-MOMORCHARIN STRUCTURE AT 2.55 A


Overview

Beta-Momorcharin (Mr approximately 29 kDa) is a single-chained ribosome-inactivating protein (RIP) with a branched hexasaccharide bound to Asn51. The crystal structure of beta-momorcharin has been determined using the molecular-replacement method and refined to 2. 55 A resolution. The final structural model gave an R factor of 17. 2% and root-mean-square deviations of 0.016 A and 1.76 degrees from ideal bond lengths and bond angles, respectively. beta-Momorcharin contains nine alpha-helices, two 310 helices and three beta-sheets, and its overall structure is similar to those of other single-chained RIPs. Residues Tyr70, Tyr109, Glu158 and Arg161 are expected to define the active site of beta-momorcharin as an rRNA N-glycosidase. The oligosaccharide is linked to the protein through an N-glycosidic bond, beta-GlcNAc-(1-N)-Asn51, and stretches from the surface of the N-terminal domain far from the active site, which suggests that it should not play a role in enzymatic function. The oligosaccharide of each beta-momorcharin molecule interacts with the protein through hydrogen bonds, although in the crystals most of these are intermolecular interactions with the protein atoms in an adjacent unit cell. This is the first example of an RIP structure which provides information about the three-dimensional structure and binding site of the oligosaccharide in the active chains of RIPs.

About this Structure

1CF5 is a Single protein structure of sequence from Momordica charantia. Full crystallographic information is available from OCA.

Reference

Three-dimensional structure of beta-momorcharin at 2.55 A resolution., Yuan YR, He YN, Xiong JP, Xia ZX, Acta Crystallogr D Biol Crystallogr. 1999 Jun;55(Pt 6):1144-51. PMID:10329776 Page seeded by OCA on Fri May 2 12:39:54 2008

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