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| - | [[Image:1hfo.gif|left|200px]] | |
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| - | {{Structure
| + | ==The Structure of the Macrophage Migration Inhibitory Factor from Trichinella Spiralis.== |
| - | |PDB= 1hfo |SIZE=350|CAPTION= <scene name='initialview01'>1hfo</scene>, resolution 1.65Å
| + | <StructureSection load='1hfo' size='340' side='right'caption='[[1hfo]], [[Resolution|resolution]] 1.65Å' scene=''> |
| - | |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>
| + | == Structural highlights == |
| - | |LIGAND= <scene name='pdbligand=UNK:UNKNOWN'>UNK</scene>
| + | <table><tr><td colspan='2'>[[1hfo]] is a 6 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HFO FirstGlance]. <br> |
| - | |ACTIVITY=
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65Å</td></tr> |
| - | |GENE=
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hfo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hfo OCA], [https://pdbe.org/1hfo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hfo RCSB], [https://www.ebi.ac.uk/pdbsum/1hfo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hfo ProSAT]</span></td></tr> |
| - | |DOMAIN=
| + | </table> |
| - | |RELATEDENTRY=
| + | == Function == |
| - | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hfo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hfo OCA], [http://www.ebi.ac.uk/pdbsum/1hfo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hfo RCSB]</span>
| + | [https://www.uniprot.org/uniprot/MIFH_TRISP MIFH_TRISP] Tautomerization of the methyl ester of L-dopachrome. Inhibits migration of human peripheral blood mononuclear cells.<ref>PMID:11439086</ref> <ref>PMID:9794786</ref> |
| - | }}
| + | == Evolutionary Conservation == |
| | + | [[Image:Consurf_key_small.gif|200px|right]] |
| | + | Check<jmol> |
| | + | <jmolCheckbox> |
| | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hf/1hfo_consurf.spt"</scriptWhenChecked> |
| | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | + | <text>to colour the structure by Evolutionary Conservation</text> |
| | + | </jmolCheckbox> |
| | + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1hfo ConSurf]. |
| | + | <div style="clear:both"></div> |
| | + | <div style="background-color:#fffaf0;"> |
| | + | == Publication Abstract from PubMed == |
| | + | 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. |
| | | | |
| - | '''THE STRUCTURE OF THE MACROPHAGE MIGRATION INHIBITORY FACTOR FROM TRICHINELLA SPIRALIS.'''
| + | 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<ref>PMID:11439086</ref> |
| | | | |
| | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | + | </div> |
| | + | <div class="pdbe-citations 1hfo" style="background-color:#fffaf0;"></div> |
| | | | |
| - | ==Overview== | + | ==See Also== |
| - | 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.
| + | *[[Macrophage inhibitory factor 3D structures|Macrophage inhibitory factor 3D structures]] |
| - | | + | == References == |
| - | ==About this Structure== | + | <references/> |
| - | 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].
| + | __TOC__ |
| - | | + | </StructureSection> |
| - | ==Reference==
| + | [[Category: Large Structures]] |
| - | 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: Trichinella spiralis]] | | [[Category: Trichinella spiralis]] |
| - | [[Category: Meyer, D J.]] | + | [[Category: Meyer DJ]] |
| - | [[Category: Roe, S M.]] | + | [[Category: Roe SM]] |
| - | [[Category: tautomerase]]
| + | |
| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:04:11 2008''
| + | |
| Structural highlights
Function
MIFH_TRISP Tautomerization of the methyl ester of L-dopachrome. Inhibits migration of human peripheral blood mononuclear cells.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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. Macrophage migration inhibitory factor of the parasitic nematode Trichinella spiralis. Biochem J. 2001 Jul 15;357(Pt 2):373-83. PMID:11439086
- ↑ Pennock JL, Behnke JM, Bickle QD, Devaney E, Grencis RK, Isaac RE, Joshua GW, Selkirk ME, Zhang Y, Meyer DJ. Rapid purification and characterization of L-dopachrome-methyl ester tautomerase (macrophage-migration-inhibitory factor) from Trichinella spiralis, Trichuris muris and Brugia pahangi. Biochem J. 1998 Nov 1;335 ( Pt 3):495-8. PMID:9794786
- ↑ 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. Macrophage migration inhibitory factor of the parasitic nematode Trichinella spiralis. Biochem J. 2001 Jul 15;357(Pt 2):373-83. PMID:11439086
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