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3uvj

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Crystal structure of the catalytic domain of the heterodimeric human soluble guanylate cyclase 1.

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 ==Crystal structure of the catalytic domain of the heterodimeric human soluble guanylate cyclase 1.==
-<StructureSection load='3uvj' size='340' side='right' caption='[[3uvj]], [[Resolution|resolution]] 2.08&Aring;' scene=''>
+<StructureSection load='3uvj' size='340' side='right'caption='[[3uvj]], [[Resolution|resolution]] 2.08&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3uvj]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UVJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UVJ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3uvj]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UVJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UVJ FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 2.08&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2wz1|2wz1]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GUC1A3, GUCSA3, GUCY1A1, GUCY1A3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), GUCY1B3, GUC1B3, GUCSB3, GUCY1B1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3uvj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uvj OCA], [https://pdbe.org/3uvj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uvj RCSB], [https://www.ebi.ac.uk/pdbsum/3uvj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uvj 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/Guanylate_cyclase Guanylate cyclase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.6.1.2 4.6.1.2] </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=3uvj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uvj OCA], [http://pdbe.org/3uvj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3uvj RCSB], [http://www.ebi.ac.uk/pdbsum/3uvj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3uvj ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Disease ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/GCYA1_HUMAN GCYA1_HUMAN] Moyamoya disease with early-onset achalasia. The disease is caused by mutations affecting the gene represented in this entry.
-Soluble guanylate cyclase (sGC) catalyses the synthesis of cyclic GMP in response to nitric oxide. The enzyme is a heterodimer of homologous alpha and beta subunits, each of which is composed of multiple domains. We present here crystal structures of a heterodimer of the catalytic domains of the alpha and beta subunits, as well as an inactive homodimer of beta subunits. This first structure of a metazoan, heteromeric cyclase provides several observations. First, the structures resemble known structures of adenylate cyclases and other guanylate cyclases in overall fold and in the arrangement of conserved active-site residues, which are contributed by both subunits at the interface. Second, the subunit interaction surface is promiscuous, allowing both homodimeric and heteromeric association; the preference of the full-length enzyme for heterodimer formation must derive from the combined contribution of other interaction interfaces. Third, the heterodimeric structure is in an inactive conformation, but can be superposed onto an active conformation of adenylate cyclase by a structural transition involving a 26 degrees rigid-body rotation of the alpha subunit. In the modelled active conformation, most active site residues in the subunit interface are precisely aligned with those of adenylate cyclase. Finally, the modelled active conformation also reveals a cavity related to the active site by pseudo-symmetry. The pseudosymmetric site lacks key active site residues, but may bind allosteric regulators in a manner analogous to the binding of forskolin to adenylate cyclase. This indicates the possibility of developing a new class of small-molecule modulators of guanylate cyclase activity targeting the catalytic domain.
+== Function ==
+[https://www.uniprot.org/uniprot/GCYA1_HUMAN GCYA1_HUMAN]
-Crystal structures of the catalytic domain of human soluble guanylate cyclase.,Allerston CK, von Delft F, Gileadi O PLoS One. 2013;8(3):e57644. doi: 10.1371/journal.pone.0057644. Epub 2013 Mar 7. PMID:23505436<ref>PMID:23505436</ref>
+==See Also==
+*[[Guanylate cyclase 3D structures|Guanylate cyclase 3D structures]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3uvj" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Guanylate cyclase]]
+[[Category: Homo sapiens]]
-[[Category: Human]]
+[[Category: Large Structures]]
-[[Category: Allerston, C K]]
+[[Category: Allerston CK]]
-[[Category: Arrowsmith, C H]]
+[[Category: Arrowsmith CH]]
-[[Category: Berridge, G]]
+[[Category: Berridge G]]
-[[Category: Bountra, C]]
+[[Category: Bountra C]]
-[[Category: Chalk, R]]
+[[Category: Chalk R]]
-[[Category: Cooper, C D.O]]
+[[Category: Cooper CDO]]
-[[Category: Delft, F von]]
+[[Category: Edwards A]]
-[[Category: Edwards, A]]
+[[Category: Gileadi O]]
-[[Category: Gileadi, O]]
+[[Category: Savitsky P]]
-[[Category: Structural genomic]]
+[[Category: Vollmar M]]
-[[Category: Savitsky, P]]
+[[Category: Weigelt J]]
-[[Category: Vollmar, M]]
+[[Category: Von Delft F]]
-[[Category: Weigelt, J]]
-[[Category: Cgmp biosynthesis]]
-[[Category: Cystol]]
-[[Category: Gtp binding metal-binding]]
-[[Category: Lyase]]
-[[Category: Nitric oxide]]
-[[Category: Nucleotide-binding]]
-[[Category: Sgc]]

3uvj

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Crystal structure of the catalytic domain of the heterodimeric human soluble guanylate cyclase 1.

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