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| | ==Mycobacterium tuberculosis adenylyl cyclase Rv1900c CHD, in complex with a substrate analog.== | | ==Mycobacterium tuberculosis adenylyl cyclase Rv1900c CHD, in complex with a substrate analog.== |
| - | <StructureSection load='1ybu' size='340' side='right' caption='[[1ybu]], [[Resolution|resolution]] 2.40Å' scene=''> | + | <StructureSection load='1ybu' size='340' side='right'caption='[[1ybu]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1ybu]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YBU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YBU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1ybu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YBU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YBU FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=APC:DIPHOSPHOMETHYLPHOSPHONIC+ACID+ADENOSYL+ESTER'>APC</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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]] 2.4Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ybt|1ybt]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=APC:DIPHOSPHOMETHYLPHOSPHONIC+ACID+ADENOSYL+ESTER'>APC</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Rv1900c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</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=1ybu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ybu OCA], [https://pdbe.org/1ybu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ybu RCSB], [https://www.ebi.ac.uk/pdbsum/1ybu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ybu 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/Adenylate_cyclase Adenylate cyclase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.6.1.1 4.6.1.1] </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=1ybu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ybu OCA], [http://pdbe.org/1ybu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ybu RCSB], [http://www.ebi.ac.uk/pdbsum/1ybu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ybu ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/O07732_MYCTU O07732_MYCTU] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Adenylyl cyclase|Adenylyl cyclase]] | + | *[[3D Adenylyl cyclase 3D structures|3D Adenylyl cyclase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Adenylate cyclase]] | + | [[Category: Large Structures]] |
| - | [[Category: Myctu]] | + | [[Category: Mycobacterium tuberculosis H37Rv]] |
| - | [[Category: Linder, J U]] | + | [[Category: Linder JU]] |
| - | [[Category: Schultz, J E]] | + | [[Category: Schultz JE]] |
| - | [[Category: Sinha, S C]] | + | [[Category: Sinha SC]] |
| - | [[Category: Sprang, S R]] | + | [[Category: Sprang SR]] |
| - | [[Category: Wetterer, M]] | + | [[Category: Wetterer M]] |
| - | [[Category: Chd]]
| + | |
| - | [[Category: Cyclase homology domain]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Rv1900c]]
| + | |
| Structural highlights
Function
O07732_MYCTU
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Rv1900c, a Mycobacterium tuberculosis adenylyl cyclase, is composed of an N-terminal alpha/beta-hydrolase domain and a C-terminal cyclase homology domain. It has an unusual 7% guanylyl cyclase side-activity. A canonical substrate-defining lysine and a catalytic asparagine indispensable for mammalian adenylyl cyclase activity correspond to N342 and H402 in Rv1900c. Mutagenic analysis indicates that these residues are dispensable for activity of Rv1900c. Structures of the cyclase homology domain, solved to 2.4 A both with and without an ATP analog, form isologous, but asymmetric homodimers. The noncanonical N342 and H402 do not interact with the substrate. Subunits of the unliganded open dimer move substantially upon binding substrate, forming a closed dimer similar to the mammalian cyclase heterodimers, in which one interfacial active site is occupied and the quasi-dyad-related active site is occluded. This asymmetry indicates that both active sites cannot simultaneously be catalytically active. Such a mechanism of half-of-sites-reactivity suggests that mammalian heterodimeric adenylyl cyclases may have evolved from gene duplication of a primitive prokaryote-type cyclase, followed by loss of function in one active site.
Origin of asymmetry in adenylyl cyclases: structures of Mycobacterium tuberculosis Rv1900c.,Sinha SC, Wetterer M, Sprang SR, Schultz JE, Linder JU EMBO J. 2005 Feb 23;24(4):663-73. Epub 2005 Jan 27. PMID:15678099[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sinha SC, Wetterer M, Sprang SR, Schultz JE, Linder JU. Origin of asymmetry in adenylyl cyclases: structures of Mycobacterium tuberculosis Rv1900c. EMBO J. 2005 Feb 23;24(4):663-73. Epub 2005 Jan 27. PMID:15678099
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