5bk2: Difference between revisions
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==Crystal structure of maltose binding protein in complex with a peristeric synthetic antibody== | ==Crystal structure of maltose binding protein in complex with a peristeric synthetic antibody== | ||
<StructureSection load='5bk2' size='340' side='right' caption='[[5bk2]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='5bk2' size='340' side='right'caption='[[5bk2]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5bk2]] is a 6 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5bk2]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BK2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BK2 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand= | </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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=5bk2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bk2 OCA], [https://pdbe.org/5bk2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5bk2 RCSB], [https://www.ebi.ac.uk/pdbsum/5bk2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5bk2 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 5bk2" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5bk2" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Maltose-binding protein 3D structures|Maltose-binding protein 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli K-12]] | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Kossiakoff AA]] | ||
[[Category: | [[Category: Mukherjee S]] | ||
Revision as of 09:42, 31 May 2023
Crystal structure of maltose binding protein in complex with a peristeric synthetic antibodyCrystal structure of maltose binding protein in complex with a peristeric synthetic antibody
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 PubMedConformational changes in proteins due to ligand binding are ubiquitous in biological systems and are integral to many biological systems. However, it is often challenging to link ligand-induced conformational changes to a resulting biological function because it is difficult to distinguish between the energetic components associated with ligand-binding and those due to structural rearrangements. Here, we used a unique approach exploiting conformation-specific and regio-specific synthetic antibodies (sABs) to probe the energetic contributions of ligand-binding to conformation changes. Using maltose binding protein (MBP) as a model system, customized phage display selections were performed to generate sABs that stabilize MBP in different conformational states, modulating ligand binding affinity in competitive, allosteric or peristeric manners. We determined that the binding of a closed conformation-specific sAB (sAB-11M) to MBP in the absence of maltose is entropically driven, providing new insight into designing antibody stabilized protein interactions. Crystal structures of sABs bound to MBP, together with biophysical data delineate the basis of free energy differences between different conformational states and confirm the use of the sABs as energy probes for dissecting enthalpic and entropic contributions to conformational transitions. Our work provides a foundation for investigating the energetic contributions of distinct conformational dynamics to specific biological outputs. We anticipate that our approach also may be valuable for analyzing the energy landscapes of regulatory proteins controlling biological responses to environmental changes. Engineered synthetic antibodies as probes to quantify the energetic contributions of ligand binding to conformational changes in proteins.,Mukherjee S, Griffin DH, Horn JR, Rizk SS, Nocula-Lugowska M, Malmqvist M, Kim SS, Kossiakoff AA J Biol Chem. 2018 Jan 10. pii: RA117.000656. doi: 10.1074/jbc.RA117.000656. PMID:29321208[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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