4a2c
From Proteopedia
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| - | [[ | + | ==Crystal structure of galactitol-1-phosphate dehydrogenase from Escherichia coli== |
| + | <StructureSection load='4a2c' size='340' side='right' caption='[[4a2c]], [[Resolution|resolution]] 1.87Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4a2c]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A2C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4A2C FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Galactitol-1-phosphate_5-dehydrogenase Galactitol-1-phosphate 5-dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.251 1.1.1.251] </span></td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4a2c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a2c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4a2c RCSB], [http://www.ebi.ac.uk/pdbsum/4a2c PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Endogenous galactitol-1-phosphate 5-dehydrogenase (GPDH) (EC 1.1.1.251) from Escherichia coli spontaneously interacts with Ni(2+)-NTA matrices becoming a potential contaminant for recombinant, target His-tagged proteins. Purified recombinant, untagged GPDH (rGPDH) converted galactitol into tagatose, and d-tagatose-6-phosphate into galactitol-1-phosphate, in a Zn(2+)- and NAD(H)-dependent manner and readily crystallized what has permitted to solve its crystal structure. In contrast, N-terminally His-tagged GPDH was marginally stable and readily aggregated. The structure of rGPDH revealed metal-binding sites characteristic from the medium-chain dehydrogenase/reductase protein superfamily which may explain its ability to interact with immobilized metals. The structure also provides clues on the harmful effects of the N-terminal His-tag. STRUCTURED SUMMARY OF PROTEIN INTERACTIONS: GPDH and GPDHbind by molecular sieving (View interaction) GPDH and GPDHbind by x-ray crystallography(View interaction) GPDH and GPDHbind by cosedimentation in solution (View interaction). | ||
| - | + | The crystal structure of galactitol-1-phosphate 5-dehydrogenase from Escherichia coli K12 provides insights into its anomalous behavior on IMAC processes.,Esteban-Torres M, Alvarez Y, Acebron I, Rivas Bde L, Munoz R, Kohring GW, Roa AM, Sobrino M, Mancheno JM FEBS Lett. 2012 Sep 21;586(19):3127-33. doi: 10.1016/j.febslet.2012.07.073. Epub , 2012 Aug 8. PMID:22979983<ref>PMID:22979983</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | == | + | __TOC__ |
| - | + | </StructureSection> | |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Galactitol-1-phosphate 5-dehydrogenase]] | [[Category: Galactitol-1-phosphate 5-dehydrogenase]] | ||
Revision as of 07:43, 9 July 2014
Crystal structure of galactitol-1-phosphate dehydrogenase from Escherichia coli
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