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1b3e
From Proteopedia
(New page: 200px<br /> <applet load="1b3e" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b3e, resolution 2.5Å" /> '''HUMAN SERUM TRANSFER...) |
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| - | [[Image:1b3e.gif|left|200px]]<br /> | + | [[Image:1b3e.gif|left|200px]]<br /><applet load="1b3e" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1b3e" size=" | + | |
caption="1b3e, resolution 2.5Å" /> | caption="1b3e, resolution 2.5Å" /> | ||
'''HUMAN SERUM TRANSFERRIN, N-TERMINAL LOBE, EXPRESSED IN PICHIA PASTORIS'''<br /> | '''HUMAN SERUM TRANSFERRIN, N-TERMINAL LOBE, EXPRESSED IN PICHIA PASTORIS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The ferric form of the N-lobe of human serum transferrin (Fe(III)-hTF/2N) | + | 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== | ==Disease== | ||
| Line 11: | Line 10: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1B3E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with FE and CO3 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1B3E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=FE:'>FE</scene> and <scene name='pdbligand=CO3:'>CO3</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B3E OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Baker, E | + | [[Category: Baker, E N.]] |
| - | [[Category: Bewley, M | + | [[Category: Bewley, M C.]] |
[[Category: Grewal, J.]] | [[Category: Grewal, J.]] | ||
[[Category: He, S.]] | [[Category: He, S.]] | ||
| - | [[Category: Macgillivray, R | + | [[Category: Macgillivray, R T.A.]] |
| - | [[Category: Mason, A | + | [[Category: Mason, A B.]] |
| - | [[Category: Murphy, M | + | [[Category: Murphy, M E.P.]] |
[[Category: Shewry, S.]] | [[Category: Shewry, S.]] | ||
| - | [[Category: Tam, B | + | [[Category: Tam, B M.]] |
| - | [[Category: Woodworth, R | + | [[Category: Woodworth, R C.]] |
[[Category: CO3]] | [[Category: CO3]] | ||
[[Category: FE]] | [[Category: FE]] | ||
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[[Category: transferrin]] | [[Category: transferrin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:51:07 2008'' |
Revision as of 09:51, 21 February 2008
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HUMAN SERUM TRANSFERRIN, N-TERMINAL LOBE, EXPRESSED IN PICHIA PASTORIS
Contents |
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 with and as ligands. 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 Thu Feb 21 11:51:07 2008
Categories: Homo sapiens | Single protein | Baker, E N. | Bewley, M C. | Grewal, J. | He, S. | Macgillivray, R T.A. | Mason, A B. | Murphy, M E.P. | Shewry, S. | Tam, B M. | Woodworth, R C. | CO3 | FE | Glycoprotein | Glycosylation | Iron transport | Pichia pastoris | Transferrin
