1b3e

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[[Image:1b3e.gif|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1b3e", creates the "Structure Box" on the page.
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|LIGAND= <scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>
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{{STRUCTURE_1b3e| PDB=1b3e | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b3e OCA], [http://www.ebi.ac.uk/pdbsum/1b3e PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1b3e RCSB]</span>
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'''HUMAN SERUM TRANSFERRIN, N-TERMINAL LOBE, EXPRESSED IN PICHIA PASTORIS'''
'''HUMAN SERUM TRANSFERRIN, N-TERMINAL LOBE, EXPRESSED IN PICHIA PASTORIS'''
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[[Category: Tam, B M.]]
[[Category: Tam, B M.]]
[[Category: Woodworth, R C.]]
[[Category: Woodworth, R C.]]
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[[Category: glycoprotein]]
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[[Category: Glycoprotein]]
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[[Category: glycosylation]]
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[[Category: Glycosylation]]
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[[Category: iron transport]]
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[[Category: Iron transport]]
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[[Category: pichia pastori]]
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[[Category: Pichia pastori]]
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[[Category: transferrin]]
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[[Category: Transferrin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:52:45 2008''
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Revision as of 08:00, 2 May 2008

Image:1b3e.gif

Template:STRUCTURE 1b3e

HUMAN SERUM TRANSFERRIN, N-TERMINAL LOBE, EXPRESSED IN PICHIA PASTORIS


Overview

The ferric form of the N-lobe of human serum transferrin (Fe(III)-hTF/2N) has been expressed at high levels in Pichia pastoris. The Fe(III)-hTF/2N was crystallized in the space group P41212, and X-ray crystallography was used to solve the structure of the recombinant protein at 2.5 A resolution. This represents only the second P. pastoris-derived protein structure determined to date, and allows the comparison of the structures of recombinant Fe(III)-hTF/2N expressed in P. pastoris and mammalian cells with serum-derived transferrin. The polypeptide folding pattern is essentially identical in all of the three proteins. Mass spectroscopic analyses of P. pastoris- hTF/2N and proteolytically derived fragments revealed glycosylation of Ser-32 with a single hexose. This represents the first localization of an O-linked glycan in a P. pastoris-derived protein. Because of its distance from the iron-binding site, glycosylation of Ser-32 should not affect the iron-binding properties of hTF/2N expressed in P. pastoris, making this an excellent expression system for the production of hTF/2N.

About this Structure

1B3E is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

X-ray crystallography and mass spectroscopy reveal that the N-lobe of human transferrin expressed in Pichia pastoris is folded correctly but is glycosylated on serine-32., Bewley MC, Tam BM, Grewal J, He S, Shewry S, Murphy ME, Mason AB, Woodworth RC, Baker EN, MacGillivray RT, Biochemistry. 1999 Feb 23;38(8):2535-41. PMID:10029548 Page seeded by OCA on Fri May 2 11:00:53 2008

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