6d66

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'''Unreleased structure'''
 
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The entry 6d66 is ON HOLD until Paper Publication
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==Crystal structure of the human dual specificity 1 catalytic domain (C258S) as a maltose binding protein fusion in complex with the designed AR protein mbp3_16==
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<StructureSection load='6d66' size='340' side='right' caption='[[6d66]], [[Resolution|resolution]] 2.23&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6d66]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6D66 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6D66 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<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=6d66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6d66 OCA], [http://pdbe.org/6d66 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6d66 RCSB], [http://www.ebi.ac.uk/pdbsum/6d66 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6d66 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[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.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors:
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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>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6d66" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Gumpena, R]]
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[[Category: Lountos, G T]]
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[[Category: Waugh, D S]]
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[[Category: C258]]
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[[Category: Darpin]]
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[[Category: Dusp]]
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[[Category: Hydrolase]]
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[[Category: Mbp]]

Revision as of 19:48, 19 September 2018

Crystal structure of the human dual specificity 1 catalytic domain (C258S) as a maltose binding protein fusion in complex with the designed AR protein mbp3_16

6d66, resolution 2.23Å

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