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| | ==Synechocystis sp. PCC 6803 1,4-dihydroxy-2-naphthoyl-coenzyme A synthase (MenB) in complex with salicylyl-CoA== | | ==Synechocystis sp. PCC 6803 1,4-dihydroxy-2-naphthoyl-coenzyme A synthase (MenB) in complex with salicylyl-CoA== |
| - | <StructureSection load='4i4z' size='340' side='right' caption='[[4i4z]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='4i4z' size='340' side='right'caption='[[4i4z]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4i4z]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/Syny3 Syny3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4I4Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4I4Z FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4i4z]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803_substr._Kazusa Synechocystis sp. PCC 6803 substr. Kazusa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4I4Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4I4Z FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2NE:SALICYLYL+COA'>2NE</scene>, <scene name='pdbligand=BCT:BICARBONATE+ION'>BCT</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</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]] 2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4eml|4eml]], [[4i52|4i52]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2NE:SALICYLYL+COA'>2NE</scene>, <scene name='pdbligand=BCT:BICARBONATE+ION'>BCT</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">menB, sll1127 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1111708 SYNY3])</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=4i4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i4z OCA], [https://pdbe.org/4i4z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4i4z RCSB], [https://www.ebi.ac.uk/pdbsum/4i4z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4i4z ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/1,4-dihydroxy-2-naphthoyl-CoA_synthase 1,4-dihydroxy-2-naphthoyl-CoA synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.36 4.1.3.36] </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=4i4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i4z OCA], [http://pdbe.org/4i4z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4i4z RCSB], [http://www.ebi.ac.uk/pdbsum/4i4z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4i4z ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/P73495_SYNY3 P73495_SYNY3] |
| | <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: 1,4-dihydroxy-2-naphthoyl-CoA synthase]] | + | [[Category: Large Structures]] |
| - | [[Category: Syny3]] | + | [[Category: Synechocystis sp. PCC 6803 substr. Kazusa]] |
| - | [[Category: Guo, Z H]] | + | [[Category: Guo ZH]] |
| - | [[Category: Jiang, M]] | + | [[Category: Jiang M]] |
| - | [[Category: Li, J]] | + | [[Category: Li J]] |
| - | [[Category: Li, Y]] | + | [[Category: Li Y]] |
| - | [[Category: Song, H G]] | + | [[Category: Song HG]] |
| - | [[Category: Sun, Y R]] | + | [[Category: Sun YR]] |
| - | [[Category: Zhou, J H]] | + | [[Category: Zhou JH]] |
| - | [[Category: 4-dihydroxy-2-naphthoyl coenzyme a synthase]]
| + | |
| - | [[Category: Crotonase]]
| + | |
| - | [[Category: Lyase]]
| + | |
| Structural highlights
Function
P73495_SYNY3
Publication Abstract from PubMed
1, 4-Dihydroxy-2-naphthoyl coenzyme A (DHNA-CoA) synthase is a typical crotonase fold enzyme with an implicated role of conformational changes in catalysis. We have identified these conformational changes by determining the structures of its Escherichia coli and Synechocystis sp. PCC6803 orthologues in complex with a product analog. The structural changes include the folding of an active-site loop into a beta-hairpin and significant reorientation of a helix at the carboxy terminus. Interestingly, a new interface is formed between the ordered loop and the reoriented helix, both of which also form additional interactions with the coenzyme A moiety of the ligand. Site-directed mutation of the amino acid residues involved in these ligand-induced interactions significantly diminishes the enzyme activity. These results suggest a catalytically essential induced-fit that is likely initiated by the enzyme-ligand interactions at the active site.
Structural basis of the induced-fit mechanism of 1,4-dihydroxy-2-naphthoyl coenzyme a synthase from the crotonase fold superfamily.,Sun Y, Song H, Li J, Li Y, Jiang M, Zhou J, Guo Z PLoS One. 2013 Apr 26;8(4):e63095. doi: 10.1371/journal.pone.0063095. Print 2013. PMID:23658663[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sun Y, Song H, Li J, Li Y, Jiang M, Zhou J, Guo Z. Structural basis of the induced-fit mechanism of 1,4-dihydroxy-2-naphthoyl coenzyme a synthase from the crotonase fold superfamily. PLoS One. 2013 Apr 26;8(4):e63095. doi: 10.1371/journal.pone.0063095. Print 2013. PMID:23658663 doi:10.1371/journal.pone.0063095
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