1b8x: Difference between revisions
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b8x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b8x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1b8x RCSB], [http://www.ebi.ac.uk/pdbsum/1b8x PDBsum]</span></td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b8x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b8x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1b8x RCSB], [http://www.ebi.ac.uk/pdbsum/1b8x PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/GST26_SCHJA GST26_SCHJA]] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] |
Revision as of 04:59, 25 December 2014
GLUTATHIONE S-TRANSFERASE FUSED WITH THE NUCLEAR MATRIX TARGETING SIGNAL OF THE TRANSCRIPTION FACTOR AML-1GLUTATHIONE S-TRANSFERASE FUSED WITH THE NUCLEAR MATRIX TARGETING SIGNAL OF THE TRANSCRIPTION FACTOR AML-1
Structural highlights
Function[GST26_SCHJA] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut. 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 PubMedA glutathione S-transferase fused with the nuclear matrix targeting signal (GST-NMTS) of AML-1/CBF-alpha2 has been crystallized by the vapor diffusion method using polyethylene glycol (PEG) as the precipitant. The NMTS is a 31-amino-acid signal peptide that can target the AML-1/CBF-alpha2 protein to the nuclear matrix. The crystal belongs to tetragonal space group P43212 with unit cell dimensions a = b = 93.4 A, c = 57.6 A. There is one GST-fusion protein per asymmetric unit. Crystals diffracted to at least 2.7 A and are appropriate for structure determination. Preliminary crystallographic study of glutathione S-transferase fused with the nuclear matrix targeting signal of the transcription factor AML-1/CBF-alpha2.,Tang L, Guo B, van Wijnen AJ, Lian JB, Stein JL, Stein GS, Zhou GW J Struct Biol. 1998 Sep;123(1):83-5. PMID:9774548[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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