1b3e: Difference between revisions
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'''HUMAN SERUM TRANSFERRIN, N-TERMINAL LOBE, EXPRESSED IN PICHIA PASTORIS''' | {{Structure | ||
|PDB= 1b3e |SIZE=350|CAPTION= <scene name='initialview01'>1b3e</scene>, resolution 2.5Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene> and <scene name='pdbligand=CO3:CARBONATE ION'>CO3</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''HUMAN SERUM TRANSFERRIN, N-TERMINAL LOBE, EXPRESSED IN PICHIA PASTORIS''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1B3E is a [ | 1B3E is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B3E OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10029548 10029548] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: glycosylation]] | [[Category: glycosylation]] | ||
[[Category: iron transport]] | [[Category: iron transport]] | ||
[[Category: pichia | [[Category: pichia pastori]] | ||
[[Category: transferrin]] | [[Category: transferrin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:05:42 2008'' | ||
Revision as of 08:05, 20 March 2008
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| 1b3e, resolution 2.5Å | |||||||||||||
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| Ligands: | FE and CO3 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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.
Disease
Known diseases associated with this structure: Atransferrinemia OMIM:[190000], Iron deficiency anemia, susceptibility to OMIM:[190000]
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
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