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| | <StructureSection load='5cee' size='340' side='right'caption='[[5cee]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='5cee' size='340' side='right'caption='[[5cee]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5cee]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aywbp Aywbp]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CEE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CEE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5cee]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aster_yellows_witches'-broom_phytoplasma_AYWB Aster yellows witches'-broom phytoplasma AYWB]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CEE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CEE FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</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]] 2.498Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sfcA, AYWB_051 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=322098 AYWBP])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Malate_dehydrogenase_(oxaloacetate-decarboxylating) Malate dehydrogenase (oxaloacetate-decarboxylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.38 1.1.1.38] </span></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=5cee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cee OCA], [https://pdbe.org/5cee PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cee RCSB], [https://www.ebi.ac.uk/pdbsum/5cee PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cee ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5cee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cee OCA], [http://pdbe.org/5cee PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cee RCSB], [http://www.ebi.ac.uk/pdbsum/5cee PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5cee ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q2NK75_AYWBP Q2NK75_AYWBP] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aywbp]] | + | [[Category: Aster yellows witches'-broom phytoplasma AYWB]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Alvarez, C E]] | + | [[Category: Alvarez CE]] |
| - | [[Category: Andreo, C S]] | + | [[Category: Andreo CS]] |
| - | [[Category: Buschiazzo, A]] | + | [[Category: Buschiazzo A]] |
| - | [[Category: Drincovich, M F]] | + | [[Category: Drincovich MF]] |
| - | [[Category: Larrieux, N]] | + | [[Category: Larrieux N]] |
| - | [[Category: Mussi, M A]] | + | [[Category: Mussi MA]] |
| - | [[Category: Saigo, M]] | + | [[Category: Saigo M]] |
| - | [[Category: Trajtenberg, F]] | + | [[Category: Trajtenberg F]] |
| - | [[Category: Malate metabolism]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Phytoplasm malic enzyme]]
| + | |
| - | [[Category: Plant pathogen]]
| + | |
| Structural highlights
Function
Q2NK75_AYWBP
Publication Abstract from PubMed
Phytoplasmas are wall-less phytopathogenic bacteria that produce devastating effects in a wide variety of plants. Reductive evolution has shaped their genome, with the loss of many genes, limiting their metabolic capacities. Owing to the high concentration of C4 compounds in plants, and the presence of malic enzyme (ME) in all phytoplasma genomes so far sequenced, the oxidative decarboxylation of L-malate might represent an adaptation to generate energy. Aster yellows witches'-broom (Candidatus Phytoplasma) ME (AYWB-ME) is one of the smallest of all characterized MEs, yet retains full enzymatic activity. Here, the crystal structure of AYWB-ME is reported, revealing a unique fold that differs from those of `canonical' MEs. AYWB-ME is organized as a dimeric species formed by intertwining of the N-terminal domains of the protomers. As a consequence of such structural differences, key catalytic residues such as Tyr36 are positioned in the active site of each protomer but are provided by the other protomer of the dimer. A Tyr36Ala mutation abolishes the catalytic activity, indicating the key importance of this residue in the catalytic process but not in the dimeric assembly. Phylogenetic analyses suggest that larger MEs (large-subunit or chimeric MEs) might have evolved from this type of smaller scaffold by gaining small sequence cassettes or an entire functional domain. The Candidatus Phytoplasma AYWB-ME structure showcases a novel minimal structure design comprising a fully functional active site, making this enzyme an attractive starting point for rational genetic design.
The crystal structure of the malic enzyme from Candidatus Phytoplasma reveals the minimal structural determinants for a malic enzyme.,Alvarez CE, Trajtenberg F, Larrieux N, Saigo M, Golic A, Andreo CS, Hogenhout SA, Mussi MA, Drincovich MF, Buschiazzo A Acta Crystallogr D Struct Biol. 2018 Apr 1;74(Pt 4):332-340. doi:, 10.1107/S2059798318002759. Epub 2018 Apr 6. PMID:29652260[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Alvarez CE, Trajtenberg F, Larrieux N, Saigo M, Golic A, Andreo CS, Hogenhout SA, Mussi MA, Drincovich MF, Buschiazzo A. The crystal structure of the malic enzyme from Candidatus Phytoplasma reveals the minimal structural determinants for a malic enzyme. Acta Crystallogr D Struct Biol. 2018 Apr 1;74(Pt 4):332-340. doi:, 10.1107/S2059798318002759. Epub 2018 Apr 6. PMID:29652260 doi:http://dx.doi.org/10.1107/S2059798318002759
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