6dtr: Difference between revisions
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<StructureSection load='6dtr' size='340' side='right'caption='[[6dtr]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='6dtr' size='340' side='right'caption='[[6dtr]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6dtr]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6dtr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DTR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6DTR FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.301Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=6dtr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dtr OCA], [https://pdbe.org/6dtr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6dtr RCSB], [https://www.ebi.ac.uk/pdbsum/6dtr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6dtr ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/G4XU73_THEMA G4XU73_THEMA] | |||
<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 6dtr" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6dtr" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Maltose-binding protein 3D structures|Maltose-binding protein 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Thermotoga maritima MSB8]] | ||
[[Category: Cuneo | [[Category: Cuneo MJ]] | ||
[[Category: Shukla | [[Category: Shukla S]] | ||
Latest revision as of 09:13, 11 October 2023
Apo T. maritima MalE3Apo T. maritima MalE3
Structural highlights
FunctionPublication Abstract from PubMedThe genome of the hyperthermophile Thermotoga maritima contains three isoforms of maltose binding protein (MBP) that are high-affinity receptors for di-, tri-, and tetrasaccharides. Two of these proteins (tmMBP1 and tmMBP2) share significant sequence identity, approximately 90%, while the third (tmMBP3) shares less than 40% identity. MBP from Escherichia coli (ecMBP) shares 35% sequence identity with the tmMBPs. This subset of MBP isoforms offers an interesting opportunity to investigate the mechanisms underlying the evolution of substrate specificity and affinity profiles in a genome where redundant MBP genes are present. In this study, the X-ray crystal structures of tmMBP1, tmMBP2, and tmMBP3 are reported in the absence and presence of oligosaccharides. tmMBP1 and tmMBP2 have binding pockets that are larger than that of tmMBP3, enabling them to bind to larger substrates, while tmMBP1 and tmMBP2 also undergo substrate-induced hinge bending motions ( approximately 52 degrees ) that are larger than that of tmMBP3 ( approximately 35 degrees ). Small-angle X-ray scattering was used to compare protein behavior in solution, and computer simulations provided insights into dynamics of these proteins. Comparing quantitative protein-substrate interactions and dynamical properties of tmMBPs with those of the promiscuous ecMBP and disaccharide selective Thermococcus litoralis MBP provides insights into the features that enable selective binding. Collectively, the results provide insights into how the structure and dynamics of tmMBP homologues enable them to differentiate between a myriad of chemical entities while maintaining their common fold. Differential Substrate Recognition by Maltose Binding Proteins Influenced by Structure and Dynamics.,Shukla S, Bafna K, Gullett C, Myles DAA, Agarwal PK, Cuneo MJ Biochemistry. 2018 Oct 9;57(40):5864-5876. doi: 10.1021/acs.biochem.8b00783. Epub, 2018 Sep 25. PMID:30204415[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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