5k06: Difference between revisions
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==Recombinant bovine beta-lactoglobulin with uncleaved N-terminal methionine (rBlgB)== | |||
<StructureSection load='5k06' size='340' side='right' caption='[[5k06]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5k06]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K06 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5K06 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</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=5k06 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k06 OCA], [http://pdbe.org/5k06 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k06 RCSB], [http://www.ebi.ac.uk/pdbsum/5k06 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k06 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/LACB_BOVIN LACB_BOVIN]] Primary component of whey, it binds retinol and is probably involved in the transport of that molecule. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Functional recombinant bovine beta-lactoglobulin has been produced by expression in E. coli using an engineered protein gene and purified to homogeneity by applying a new protocol. Mutations L1A/I2S introduced into the protein sequence greatly facilitate in vivo cleavage of the N-terminal methionine, allowing correctly folded and soluble protein suitable for biochemical, biophysical and structural studies to be obtained. The use of gel filtration on Sephadex G75 at the last purification step enables protein without endogenous ligand to be obtained. The physicochemical properties of recombinant beta-lactoglobulin such as CD spectra, ligand binding (n, K a, DeltaH, TDeltaS, DeltaG), chemical and thermal stability (DeltaG D, C mid) and crystal structure confirmed that the protein obtained is almost identical to the natural one. The substitutions of N-terminal residues did not influence the binding properties of the recombinant protein so that the lactoglobulin produced and purified according to our protocol is a good candidate for further engineering and potential use in pharmacology and medicine. | |||
Engineered beta-Lactoglobulin Produced in E. coli: Purification, Biophysical and Structural Characterisation.,Loch JI, Bonarek P, Tworzydlo M, Polit A, Hawro B, Lach A, Ludwin E, Lewinski K Mol Biotechnol. 2016 Jul 5. PMID:27380951<ref>PMID:27380951</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: | <div class="pdbe-citations 5k06" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bonarek, P]] | |||
[[Category: Hawro, B]] | [[Category: Hawro, B]] | ||
[[Category: Lach, A]] | [[Category: Lach, A]] | ||
[[Category: Loch, J | [[Category: Lewinski, K]] | ||
[[Category: Loch, J I]] | |||
[[Category: Ludwin, E]] | |||
[[Category: Polit, A]] | [[Category: Polit, A]] | ||
[[Category: | [[Category: Tworzydlo, M]] | ||
[[Category: | [[Category: Lipocalin]] | ||
[[Category: Transport protein]] | |||
Revision as of 18:12, 26 July 2016
Recombinant bovine beta-lactoglobulin with uncleaved N-terminal methionine (rBlgB)Recombinant bovine beta-lactoglobulin with uncleaved N-terminal methionine (rBlgB)
Structural highlights
Function[LACB_BOVIN] Primary component of whey, it binds retinol and is probably involved in the transport of that molecule. Publication Abstract from PubMedFunctional recombinant bovine beta-lactoglobulin has been produced by expression in E. coli using an engineered protein gene and purified to homogeneity by applying a new protocol. Mutations L1A/I2S introduced into the protein sequence greatly facilitate in vivo cleavage of the N-terminal methionine, allowing correctly folded and soluble protein suitable for biochemical, biophysical and structural studies to be obtained. The use of gel filtration on Sephadex G75 at the last purification step enables protein without endogenous ligand to be obtained. The physicochemical properties of recombinant beta-lactoglobulin such as CD spectra, ligand binding (n, K a, DeltaH, TDeltaS, DeltaG), chemical and thermal stability (DeltaG D, C mid) and crystal structure confirmed that the protein obtained is almost identical to the natural one. The substitutions of N-terminal residues did not influence the binding properties of the recombinant protein so that the lactoglobulin produced and purified according to our protocol is a good candidate for further engineering and potential use in pharmacology and medicine. Engineered beta-Lactoglobulin Produced in E. coli: Purification, Biophysical and Structural Characterisation.,Loch JI, Bonarek P, Tworzydlo M, Polit A, Hawro B, Lach A, Ludwin E, Lewinski K Mol Biotechnol. 2016 Jul 5. PMID:27380951[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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