3zc8: Difference between revisions
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==Crystal Structure of Murraya koenigii Miraculin-Like Protein at 2.2 A resolution at pH 7.0== | ==Crystal Structure of Murraya koenigii Miraculin-Like Protein at 2.2 A resolution at pH 7.0== | ||
<StructureSection load='3zc8' size='340' side='right' caption='[[3zc8]], [[Resolution|resolution]] 2.24Å' scene=''> | <StructureSection load='3zc8' size='340' side='right'caption='[[3zc8]], [[Resolution|resolution]] 2.24Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3zc8]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3zc8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Murraya_koenigii Murraya koenigii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZC8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZC8 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.24Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3zc8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zc8 OCA], [https://pdbe.org/3zc8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zc8 RCSB], [https://www.ebi.ac.uk/pdbsum/3zc8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zc8 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/D2YW43_MURKO D2YW43_MURKO] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3zc8" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Trypsin inhibitor 3D structures|Trypsin inhibitor 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Murraya koenigii]] | [[Category: Murraya koenigii]] | ||
[[Category: Kumar | [[Category: Kumar P]] | ||
[[Category: Selvakumar | [[Category: Selvakumar P]] | ||
[[Category: Sharma | [[Category: Sharma AK]] | ||
[[Category: Sharma | [[Category: Sharma N]] | ||
[[Category: Tomar | [[Category: Tomar PPS]] | ||
Latest revision as of 13:58, 20 December 2023
Crystal Structure of Murraya koenigii Miraculin-Like Protein at 2.2 A resolution at pH 7.0Crystal Structure of Murraya koenigii Miraculin-Like Protein at 2.2 A resolution at pH 7.0
Structural highlights
FunctionPublication Abstract from PubMedMurraya koenigii miraculin-like protein (MKMLP) gradually precipitates below pH 7.5. Here, we explore the basis for this aggregation by identifying the aggregation-prone regions via comparative analysis of crystal structures acquired at several pH values. The prediction of aggregation-prone regions showed the presence of four short peptides either in beta sheets or loops on surface of the protein. These peptides were distributed in two patches far apart on the surface. Comparison of crystal structures of MKMLP, determined at 2.2 A resolution in pH 7.0 and 4.6 in the present study and determined at 2.9 A in pH 8.0 in an earlier reported study, reveal subtle conformational differences resulting in gradual exposure of aggregation-prone regions. As the pH is lowered, there are alterations in ionic interactions within the protein interactions of the chain with water molecules and exposure of hydrophobic residues. The analysis of symmetry-related molecular interfaces involving one patch revealed shortening of nonpolar intermolecular contacts as the pH decreased. In particular, a decrease in the intermolecular distance between Trp103 of the aggregation-prone peptide WFITTG (103-108) unique to MLPs was observed. These results demonstrated that aggregation occurs due to the cumulative effect of the changes in interactions in two aggregation-prone defined regions. Proteins 2013. (c) 2013 Wiley Periodicals, Inc. Structural insights into the aggregation behavior of Murraya koenigii miraculin-like protein below pH 7.5.,Selvakumar P, Sharma N, Tomar PP, Kumar P, Sharma AK Proteins. 2013 Oct 30. doi: 10.1002/prot.24461. PMID:24265134[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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