1y10

<table><tr><td colspan='2'>[[1y10]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. 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 [http://proteopedia.org/fgij/fg.htm?mol=1Y10 FirstGlance]. <br>

</td></tr><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>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1y11|1y11]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Rv1264 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</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://proteopedia.org/fgij/fg.htm?mol=1y10 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y10 OCA], [http://pdbe.org/1y10 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1y10 RCSB], [http://www.ebi.ac.uk/pdbsum/1y10 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1y10 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/Y1264_MYCTU Y1264_MYCTU]] Catalyzes the formation of the second messenger cAMP.

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== Publication Abstract from PubMed ==

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.

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:15890882<ref>PMID:15890882</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1y10" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Adenylate cyclase]]

[[Category: Findeisen, F]]

[[Category: Linder, J U]]

[[Category: Schultz, A]]

[[Category: Schultz, J E]]

[[Category: Sinning, I]]

[[Category: Tews, I]]

[[Category: Lyase]]