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| | <StructureSection load='5d15' size='340' side='right'caption='[[5d15]], [[Resolution|resolution]] 1.50Å' scene=''> | | <StructureSection load='5d15' size='340' side='right'caption='[[5d15]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5d15]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_avium_subsp._avium_10-9275 Mycobacterium avium subsp. avium 10-9275]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D15 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D15 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5d15]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_avium_subsp._avium_10-9275 Mycobacterium avium subsp. avium 10-9275]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D15 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5D15 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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]] 1.5Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5d0e|5d0e]], [[5d0g|5d0g]], [[5d0h|5d0h]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">O972_06080 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1391991 Mycobacterium avium subsp. avium 10-9275])</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=5d15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d15 OCA], [https://pdbe.org/5d15 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5d15 RCSB], [https://www.ebi.ac.uk/pdbsum/5d15 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5d15 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=5d15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d15 OCA], [http://pdbe.org/5d15 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d15 RCSB], [http://www.ebi.ac.uk/pdbsum/5d15 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5d15 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Mycobacterium avium subsp. avium 10-9275]] | | [[Category: Mycobacterium avium subsp. avium 10-9275]] |
| - | [[Category: Barathy, D V]] | + | [[Category: Barathy DV]] |
| - | [[Category: Bharambe, N G]] | + | [[Category: Bharambe NG]] |
| - | [[Category: Suguna, K]] | + | [[Category: Suguna K]] |
| - | [[Category: Adenylyl cyclase]]
| + | |
| - | [[Category: Atp]]
| + | |
| - | [[Category: Lyase]]
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| Structural highlights
Publication Abstract from PubMed
The two second messengers in signaling, cyclic AMP and cyclic GMP, are produced by adenylyl and guanylyl cyclases, respectively. Recognition and discrimination of the substrates ATP and GTP by the nucleotidyl cyclases is vital in these reactions. Various apo, substrate or inhibitor bound forms of adenylyl cyclase (AC) structures from transmembrane and soluble ACs have revealed the catalytic mechanism of ATP cyclization reaction. Previously reported structures of guanylyl cyclases represent ligand-free forms and inactive open states of the enzymes and thus do not provide information regarding the exact mode of substrate binding. The structures we present here of the cyclase homology domain of a class III AC from Mycobacterium avium (Ma1120) and its mutant in complex with ATP and GTP in the presence of calcium ion, provide the structural basis for substrate selection by the nucleotidyl cyclases at the atomic level. Precise nature of the enzyme-substrate interactions, novel modes of substrate binding and the ability of the binding pocket to accommodate diverse conformations of the substrates have been revealed by the present crystallographic analysis. This is the first report to provide structures of both the nucleotide substrates bound to a nucleotidyl cyclase. This article is protected by copyright. All rights reserved.
Substrate specificity determinants of class III nucleotidyl cyclases.,Bharambe NG, Barathy DV, Syed W, Visweswariah SS, Colavarsigmao M, Misquith S, Suguna K FEBS J. 2016 Aug 20. doi: 10.1111/febs.13837. PMID:27542992[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bharambe NG, Barathy DV, Syed W, Visweswariah SS, Colavarsigmao M, Misquith S, Suguna K. Substrate specificity determinants of class III nucleotidyl cyclases. FEBS J. 2016 Aug 20. doi: 10.1111/febs.13837. PMID:27542992 doi:http://dx.doi.org/10.1111/febs.13837
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