7mch
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of a single-chain E/F type bilin lyase-isomerase MpeQ in space group C2221== | |
| + | <StructureSection load='7mch' size='340' side='right'caption='[[7mch]], [[Resolution|resolution]] 2.95Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7mch]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechococcus_sp._A15-62 Synechococcus sp. A15-62]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7MCH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7MCH 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]] 2.95Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=7mch FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7mch OCA], [https://pdbe.org/7mch PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7mch RCSB], [https://www.ebi.ac.uk/pdbsum/7mch PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7mch ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/U3MW57_9SYNE U3MW57_9SYNE] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Chromophore attachment of the light-harvesting apparatus represents one of the most important post-translational modifications in photosynthetic cyanobacteria. Extensive pigment diversity of cyanobacteria critically depends on bilin lyases that covalently attach chemically distinct chromophores to phycobiliproteins. However, how bilin lyases catalyze bilin ligation reactions and how some lyases acquire additional isomerase abilities remain elusive at the molecular level. Here, we report the crystal structure of a representative bilin lyase-isomerase MpeQ. This structure has revealed a "question-mark" protein architecture that unambiguously establishes the active site conserved among the E/F-type bilin lyases. Based on structural, mutational, and modeling data, we demonstrate that stereoselectivity of the active site plays a critical role in conferring the isomerase activity of MpeQ. We further advance a tyrosine-mediated reaction scheme unifying different types of bilin lyases. These results suggest that lyases and isomerase actions of bilin lyases arise from two coupled molecular events of distinct origin. | ||
| - | + | Crystal structure and molecular mechanism of an E/F type bilin lyase-isomerase.,Kumarapperuma I, Joseph KL, Wang C, Biju LM, Tom IP, Weaver KD, Grebert T, Partensky F, Schluchter WM, Yang X Structure. 2022 Feb 2. pii: S0969-2126(22)00007-7. doi:, 10.1016/j.str.2022.01.007. PMID:35148828<ref>PMID:35148828</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 7mch" style="background-color:#fffaf0;"></div> |
| - | [[Category: Kumarapperuma | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Synechococcus sp. A15-62]] | ||
| + | [[Category: Kumarapperuma I]] | ||
| + | [[Category: Yang X]] | ||
Current revision
Crystal structure of a single-chain E/F type bilin lyase-isomerase MpeQ in space group C2221
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