1hfo
From Proteopedia
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| - | [[Image:1hfo.gif|left|200px]] | + | [[Image:1hfo.gif|left|200px]] |
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| - | '''THE STRUCTURE OF THE MACROPHAGE MIGRATION INHIBITORY FACTOR FROM TRICHINELLA SPIRALIS.''' | + | {{Structure |
| + | |PDB= 1hfo |SIZE=350|CAPTION= <scene name='initialview01'>1hfo</scene>, resolution 1.65Å | ||
| + | |SITE= <scene name='pdbsite=DTA:Site+Of+L-Dopachrome+Methyl+Ester+Tautomerase+Activity+C+...'>DTA</scene>, <scene name='pdbsite=DTB:Site+Of+L-Dopachrome+Methyl+Ester+Tautomerase+Activity+C+...'>DTB</scene>, <scene name='pdbsite=DTC:Site+Of+L-Dopachrome+Methyl+Ester+Tautomerase+Activity+C+...'>DTC</scene>, <scene name='pdbsite=DTD:Site+Of+L-Dopachrome+Methyl+Ester+Tautomerase+Activity+C+...'>DTD</scene>, <scene name='pdbsite=DTE:Site+Of+L-Dopachrome+Methyl+Ester+Tautomerase+Activity+C+...'>DTE</scene> and <scene name='pdbsite=DTF:Site+Of+L-Dopachrome+Methyl+Ester+Tautomerase+Activity+C+...'>DTF</scene> | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''THE STRUCTURE OF THE MACROPHAGE MIGRATION INHIBITORY FACTOR FROM TRICHINELLA SPIRALIS.''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1HFO is a [ | + | 1HFO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Trichinella_spiralis Trichinella spiralis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HFO OCA]. |
==Reference== | ==Reference== | ||
| - | Macrophage migration inhibitory factor of the parasitic nematode Trichinella spiralis., Tan TH, Edgerton SA, Kumari R, McAlister MS, Roe SM, Nagl S, Pearl LH, Selkirk ME, Bianco AE, Totty NF, Engwerda C, Gray CA, Meyer DJ, Biochem J. 2001 Jul 15;357(Pt 2):373-83. PMID:[http:// | + | Macrophage migration inhibitory factor of the parasitic nematode Trichinella spiralis., Tan TH, Edgerton SA, Kumari R, McAlister MS, Roe SM, Nagl S, Pearl LH, Selkirk ME, Bianco AE, Totty NF, Engwerda C, Gray CA, Meyer DJ, Biochem J. 2001 Jul 15;357(Pt 2):373-83. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11439086 11439086] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Trichinella spiralis]] | [[Category: Trichinella spiralis]] | ||
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[[Category: tautomerase]] | [[Category: tautomerase]] | ||
| - | ''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 11:36:33 2008'' |
Revision as of 09:36, 20 March 2008
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| , resolution 1.65Å | |||||||
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| Sites: | , , , , and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE STRUCTURE OF THE MACROPHAGE MIGRATION INHIBITORY FACTOR FROM TRICHINELLA SPIRALIS.
Overview
cDNAs were obtained for macrophage migration-inhibitory factor (MIF)/L-dopachrome methyl ester tautomerase homologues from the parasitic nematodes Trichinella spiralis (TsMIF) and Trichuris trichiura (TtMIF). The translated sequences, which were partly confirmed by sequencing of proteolytic fragments, show 42 and 44% identity respectively with human or mouse MIF, and are shorter by one C-terminal residue. Unlike vertebrate MIF and MIF homologues of filarial nematodes, neither TsMIF nor TtMIF contain cysteine residues. Soluble recombinant TsMIF, expressed in Escherichia coli showed secondary structure (by CD spectroscopy) and quaternary structure (by light-scattering and gel filtration) similar to that of the trimeric mammalian MIFs and D-dopachrome tautomerase. The catalytic specificity of recombinant TsMIF in the ketonization of phenylpyruvate (1.4x10(6) M(-1) x s(-1)) was comparable with that of human MIF, while that of p-hydroxyphenylpyruvate (9.1x10(4) M(-1) x s(-1)) was 71-fold lower. TsMIF showed high specificity in tautomerization of the methyl ester of L-dopachrome compared with non-esterified L-dopachrome (>87000-fold) and a high kcat (approximately 4x10(4) s(-1). The crystal structure, determined to 1.65 A (1 A=0.1 nm), was generally similar to that of human MIF, but differed in the boundaries of the putative active-site pocket, which can explain the low activity towards p-hydroxyphenylpyruvate. The central pore was blocked, but was continuous, with the three putative tautomerase sites. Recombinant TsMIF (5 ng/ml-5 pg/ml) inhibited migration of human peripheral-blood mononuclear cells in a manner similar to that shown by human MIF, but had no effect from 5 to 500 ng/ml on anti-CD3-stimulated murine T-cell proliferation. TsMIF was detected in supernatants of T. spiralis larvae cultured in vitro at 6 ng/ml (55 ng/mg total secreted protein). In conclusion TsMIF has structural, catalytic and cell-migration-inhibitory properties which indicate that it is partially orthologous to mammalian MIF.
About this Structure
1HFO is a Single protein structure of sequence from Trichinella spiralis. Full crystallographic information is available from OCA.
Reference
Macrophage migration inhibitory factor of the parasitic nematode Trichinella spiralis., Tan TH, Edgerton SA, Kumari R, McAlister MS, Roe SM, Nagl S, Pearl LH, Selkirk ME, Bianco AE, Totty NF, Engwerda C, Gray CA, Meyer DJ, Biochem J. 2001 Jul 15;357(Pt 2):373-83. PMID:11439086
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