1ybu

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{{Seed}}
 
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[[Image:1ybu.png|left|200px]]
 
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==Mycobacterium tuberculosis adenylyl cyclase Rv1900c CHD, in complex with a substrate analog.==
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The line below this paragraph, containing "STRUCTURE_1ybu", creates the "Structure Box" on the page.
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<StructureSection load='1ybu' size='340' side='right'caption='[[1ybu]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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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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or leave the SCENE parameter empty for the default display.
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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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<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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{{STRUCTURE_1ybu| PDB=1ybu | SCENE= }}
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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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== Function ==
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[https://www.uniprot.org/uniprot/O07732_MYCTU O07732_MYCTU]
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== Evolutionary Conservation ==
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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 ==
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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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===Mycobacterium tuberculosis adenylyl cyclase Rv1900c CHD, in complex with a substrate analog.===
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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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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1ybu" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_15678099}}, adds the Publication Abstract to the page
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*[[3D Adenylyl cyclase 3D structures|3D Adenylyl cyclase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 15678099 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15678099}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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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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[[Category: Mycobacterium tuberculosis H37Rv]]
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[[Category: Linder JU]]
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==Reference==
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[[Category: Schultz JE]]
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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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[[Category: Sinha SC]]
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[[Category: Adenylate cyclase]]
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[[Category: Sprang SR]]
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[[Category: Mycobacterium tuberculosis h37rv]]
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[[Category: Wetterer M]]
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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: 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 Mon Jul 28 13:14:23 2008''
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Current revision

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

PDB ID 1ybu

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