6d65: Difference between revisions
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==Crystal structure of the human dual specificity phosphatase 1 catalytic domain (C258S) as a maltose binding protein fusion in complex with the designed AR protein off7== | |||
<StructureSection load='6d65' size='340' side='right' caption='[[6d65]], [[Resolution|resolution]] 2.35Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6d65]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6D65 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6D65 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EOH:ETHANOL'>EOH</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=6d65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6d65 OCA], [http://pdbe.org/6d65 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6d65 RCSB], [http://www.ebi.ac.uk/pdbsum/6d65 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6d65 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI]] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The production of high-quality crystals is the main bottleneck in determining the structures of proteins using X-ray crystallography. In addition to being recognized as a very effective solubility-enhancing fusion partner, Escherichia coli maltose-binding protein (MBP) has also been successfully employed as a `fixed-arm' crystallization chaperone in more than 100 cases. Here, it is reported that designed ankyrin-repeat proteins (DARPins) that bind with high affinity to MBP can promote the crystallization of an MBP fusion protein when the fusion protein alone fails to produce diffraction-quality crystals. As a proof of principle, three different co-crystal structures of MBP fused to the catalytic domain of human dual-specificity phosphatase 1 in complex with DARPins are reported. | |||
MBP-binding DARPins facilitate the crystallization of an MBP fusion protein.,Gumpena R, Lountos GT, Waugh DS Acta Crystallogr F Struct Biol Commun. 2018 Sep 1;74(Pt 9):549-557. doi:, 10.1107/S2053230X18009901. Epub 2018 Aug 29. PMID:30198887<ref>PMID:30198887</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6d65" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Gumpena, R]] | |||
[[Category: Lountos, G T]] | |||
[[Category: Waugh, D S]] | |||
[[Category: C258]] | |||
[[Category: Darpin]] | |||
[[Category: Dual specificity phosphatase]] | |||
[[Category: Dusp]] | |||
[[Category: Hydrolase]] | |||
[[Category: Mbp]] | |||
Revision as of 22:48, 19 September 2018
Crystal structure of the human dual specificity phosphatase 1 catalytic domain (C258S) as a maltose binding protein fusion in complex with the designed AR protein off7Crystal structure of the human dual specificity phosphatase 1 catalytic domain (C258S) as a maltose binding protein fusion in complex with the designed AR protein off7
Structural highlights
Function[MALE_ECOLI] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides. Publication Abstract from PubMedThe production of high-quality crystals is the main bottleneck in determining the structures of proteins using X-ray crystallography. In addition to being recognized as a very effective solubility-enhancing fusion partner, Escherichia coli maltose-binding protein (MBP) has also been successfully employed as a `fixed-arm' crystallization chaperone in more than 100 cases. Here, it is reported that designed ankyrin-repeat proteins (DARPins) that bind with high affinity to MBP can promote the crystallization of an MBP fusion protein when the fusion protein alone fails to produce diffraction-quality crystals. As a proof of principle, three different co-crystal structures of MBP fused to the catalytic domain of human dual-specificity phosphatase 1 in complex with DARPins are reported. MBP-binding DARPins facilitate the crystallization of an MBP fusion protein.,Gumpena R, Lountos GT, Waugh DS Acta Crystallogr F Struct Biol Commun. 2018 Sep 1;74(Pt 9):549-557. doi:, 10.1107/S2053230X18009901. Epub 2018 Aug 29. PMID:30198887[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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