1ybu

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[[Image:1ybu.gif|left|200px]]
 
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{{Structure
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==Mycobacterium tuberculosis adenylyl cyclase Rv1900c CHD, in complex with a substrate analog.==
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|PDB= 1ybu |SIZE=350|CAPTION= <scene name='initialview01'>1ybu</scene>, resolution 2.40&Aring;
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<StructureSection load='1ybu' size='340' side='right'caption='[[1ybu]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> and <scene name='pdbligand=APC:DIPHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER'>APC</scene>
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<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>
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|ACTIVITY= [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]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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|GENE= Rv1900c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 Mycobacterium tuberculosis H37Rv])
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<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>
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}}
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<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>
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</table>
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'''Mycobacterium tuberculosis adenylyl cyclase Rv1900c CHD, in complex with a substrate analog.'''
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== Function ==
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[https://www.uniprot.org/uniprot/O07732_MYCTU O07732_MYCTU]
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yb/1ybu_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ybu ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== 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.
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.
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==About this Structure==
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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<ref>PMID:15678099</ref>
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1YBU is a [[Single protein]] structure of sequence from [http://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].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15678099 15678099]
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</div>
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[[Category: Adenylate cyclase]]
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<div class="pdbe-citations 1ybu" style="background-color:#fffaf0;"></div>
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[[Category: Mycobacterium tuberculosis h37rv]]
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[[Category: Single protein]]
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[[Category: Linder, J U.]]
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[[Category: Schultz, J E.]]
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[[Category: Sinha, S C.]]
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[[Category: Sprang, S R.]]
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[[Category: Wetterer, M.]]
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[[Category: APC]]
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[[Category: MN]]
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[[Category: chd]]
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[[Category: cyclase homology domain]]
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[[Category: rv1900c]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:20:52 2008''
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==See Also==
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*[[3D Adenylyl cyclase 3D structures|3D Adenylyl cyclase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Mycobacterium tuberculosis H37Rv]]
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[[Category: Linder JU]]
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[[Category: Schultz JE]]
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[[Category: Sinha SC]]
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[[Category: Sprang SR]]
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[[Category: Wetterer M]]

Current revision

Mycobacterium tuberculosis adenylyl cyclase Rv1900c CHD, in complex with a substrate analog.

PDB ID 1ybu

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