1y10

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(New page: 200px<br /><applet load="1y10" size="450" color="white" frame="true" align="right" spinBox="true" caption="1y10, resolution 2.30&Aring;" /> '''Mycobacterial adenyl...)
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[[Image:1y10.gif|left|200px]]<br /><applet load="1y10" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1y10, resolution 2.30&Aring;" />
 
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'''Mycobacterial adenylyl cyclase Rv1264, holoenzyme, inhibited state'''<br />
 
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==Overview==
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==Mycobacterial adenylyl cyclase Rv1264, holoenzyme, inhibited state==
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Class III adenylyl cyclases contain catalytic and regulatory domains, yet, structural insight into their interactions is missing. We show that the, mycobacterial adenylyl cyclase Rv1264 is rendered a pH sensor by its, N-terminal domain. In the structure of the inhibited state, catalytic and, regulatory domains share a large interface involving catalytic residues., In the structure of the active state, the two catalytic domains rotate by, 55 degrees to form two catalytic sites at their interface. Two alpha, helices serve as molecular switches. Mutagenesis is consistent with a, regulatory role of the structural transition, and we suggest that the, transition is regulated by pH.
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<StructureSection load='1y10' size='340' side='right'caption='[[1y10]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1y10]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y10 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y10 FirstGlance]. <br>
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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]] 2.3&#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=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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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=1y10 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y10 OCA], [https://pdbe.org/1y10 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y10 RCSB], [https://www.ebi.ac.uk/pdbsum/1y10 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y10 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Y1264_MYCTU Y1264_MYCTU] Catalyzes the formation of the second messenger cAMP.
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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/y1/1y10_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=1y10 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1Y10 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with CA and 1PE as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Y10 OCA].
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*[[3D Adenylyl cyclase 3D structures|3D Adenylyl cyclase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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The structure of a pH-sensing mycobacterial adenylyl cyclase holoenzyme., Tews I, Findeisen F, Sinning I, Schultz A, Schultz JE, Linder JU, Science. 2005 May 13;308(5724):1020-3. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15890882 15890882]
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[[Category: Large Structures]]
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[[Category: Adenylate cyclase]]
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[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]
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[[Category: Single protein]]
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[[Category: Findeisen F]]
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[[Category: Findeisen, F.]]
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[[Category: Linder JU]]
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[[Category: Linder, J.U.]]
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[[Category: Schultz A]]
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[[Category: Schultz, A.]]
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[[Category: Schultz JE]]
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[[Category: Schultz, J.E.]]
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[[Category: Sinning I]]
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[[Category: Sinning, I.]]
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[[Category: Tews I]]
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[[Category: Tews, I.]]
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[[Category: 1PE]]
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[[Category: CA]]
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[[Category: adenylyl cyclase fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:28:57 2007''
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Current revision

Mycobacterial adenylyl cyclase Rv1264, holoenzyme, inhibited state

PDB ID 1y10

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