View source for 5eha


==Crystal structure of recombinant MtaL at 1.35 Angstrom resolution==
<StructureSection load='5eha' size='340' side='right'caption='[[5eha]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5eha]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Agaricus_bisporus Agaricus bisporus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EHA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EHA FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.35&#8491;</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=5eha FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5eha OCA], [https://pdbe.org/5eha PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5eha RCSB], [https://www.ebi.ac.uk/pdbsum/5eha PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5eha ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/G1K3P4_AGABI G1K3P4_AGABI] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Mushroom tyrosinase-associated lectin-like protein (MtaL) binds to mature Agaricus bisporus tyrosinase in vivo, but the exact physiological function of MtaL is unknown. In this study, the crystal structure of recombinant MtaL is reported at 1.35 A resolution. Comparison of its structure with that of the truncated and cleaved MtaL present in the complex with tyrosinase directly isolated from mushroom shows that the general beta-trefoil fold is conserved. However, differences are detected in the loop regions, particularly in the beta2-beta3 loop, which is intact and not cleaved in the recombinant MtaL. Furthermore, the N-terminal tail is rotated inwards, covering the tyrosinase-binding interface. Thus, MtaL must undergo conformational changes in order to bind mature mushroom tyrosinase. Very interestingly, the beta-trefoil fold has been identified to be essential for carbohydrate interaction in other lectin-like proteins. Comparison of the structures of MtaL and a ricin-B-like lectin with a bound disaccharide shows that MtaL may have a similar carbohydrate-binding site that might be involved in glycoreceptor activity.

Crystal structure of recombinant tyrosinase-binding protein MtaL at 1.35 A resolution.,Lai X, Soler-Lopez M, Ismaya WT, Wichers HJ, Dijkstra BW Acta Crystallogr F Struct Biol Commun. 2016 Mar 1;72(Pt 3):244-50. doi:, 10.1107/S2053230X16002107. Epub 2016 Feb 19. PMID:26919530<ref>PMID:26919530</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5eha" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Agaricus bisporus]]
[[Category: Large Structures]]
[[Category: Dijkstra BW]]
[[Category: Lai X-L]]
[[Category: Soler-Lopez M]]
[[Category: Wichers HJ]]