7jtr: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7jtr]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7JTR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7JTR FirstGlance]. <br> | <table><tr><td colspan='2'>[[7jtr]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7JTR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7JTR FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7jtr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jtr OCA], [https://pdbe.org/7jtr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7jtr RCSB], [https://www.ebi.ac.uk/pdbsum/7jtr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7jtr ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7jtr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jtr OCA], [https://pdbe.org/7jtr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7jtr RCSB], [https://www.ebi.ac.uk/pdbsum/7jtr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7jtr ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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==See Also== | ==See Also== | ||
*[[Maltose-binding protein 3D structures|Maltose-binding protein 3D structures]] | *[[Maltose-binding protein 3D structures|Maltose-binding protein 3D structures]] | ||
*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Latest revision as of 18:11, 18 October 2023
Complex of maltose-binding protein (MBP) with single-chain Fv (scFv)Complex of maltose-binding protein (MBP) with single-chain Fv (scFv)
Structural highlights
FunctionMALE_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 PubMedMaltose binding protein (MBP) is used in recombinant protein expression as an affinity and solubility tag. The monoclonal antibody B48 binds MBP tightly and has no cross-reactivity to other proteins in an Escherichia coli lysate. This high level of specificity suggested that MBP contains an epitope that could prove useful as a purification and visualization tag for proteins expressed in E. coli. To discover the MBP epitope, a co-crystal structure was determined for MBP bound to its antibody and four amino acids of MBP were identified as critical for the binding interaction. Fusions of various fragments of MBP to the glutathione S-transferase protein were engineered in order to identify the smallest fragment still recognized by the alpha-MBP antibody. Stabilization of the epitope via mutational engineering resulted in a minimized 14 amino-acid tag. A useful epitope tag derived from maltose binding protein.,Lenon M, Ke N, Ren G, Meuser ME, Loll PJ, Riggs P, Berkmen M Protein Sci. 2021 Jun;30(6):1235-1246. doi: 10.1002/pro.4088. PMID:33896065[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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