3lah: Difference between revisions

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 <StructureSection load='3lah' size='340' side='right'caption='[[3lah]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3lah]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/As_1.2430 As 1.2430]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LAH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LAH FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3lah]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Caldanaerobacter_subterraneus_subsp._tengcongensis Caldanaerobacter subterraneus subsp. tengcongensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LAH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LAH FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</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&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1u55|1u55]], [[1u56|1u56]], [[1u4h|1u4h]], [[3eee|3eee]], [[3iqb|3iqb]], [[3lai|3lai]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Tar4, TTE0680 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=119072 AS 1.2430])</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=3lah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lah OCA], [https://pdbe.org/3lah PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lah RCSB], [https://www.ebi.ac.uk/pdbsum/3lah PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lah ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q8RBX6_CALS4 Q8RBX6_CALS4]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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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=3lah ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Nitric oxide (NO) signaling in mammals controls important processes such as smooth muscle relaxation and neurotransmission by activation of soluble guanylate cyclase (sGC). NO binding to the heme domain of sGC leads to dissociation of the iron-histidine (Fe-His) bond, which is required for enzyme activity. The heme domain of sGC belongs to a larger class of proteins called H-NOX (Heme Nitric oxide/OXygen) domains. Previous crystallographic studies on H-NOX domains demonstrate a correlation between heme bending and protein conformation. It was unclear, however, whether these structural changes were important for signal transduction. Subsequent NMR solution structures of H-NOX proteins show a conformational change, upon disconnection of the heme and proximal helix, similar to those observed in the crystallographic studies. The atomic details of these conformational changes, however, are lacking in the NMR structures especially at the heme pocket. Here, a high-resolution crystal structure of an H-NOX mutant mimicking a broken Fe-His bond is reported. This mutant exhibits specific changes in heme conformation and major N-terminal displacements relative to the wild-type H-NOX protein. Fe-His ligation is ubiquitous in all H-NOX domains, and therefore, the heme and protein conformational changes observed in the present study are likely to occur throughout the H-NOX family when NO binding leads to rupture of the Fe-His bond.
-Structural insights into the molecular mechanism of H-NOX activation.,Olea C Jr, Herzik MA Jr, Kuriyan J, Marletta MA Protein Sci. 2010 Feb 16. PMID:20162612<ref>PMID:20162612</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3lah" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
 *[[Methyl-accepting chemotaxis protein|Methyl-accepting chemotaxis protein]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: As 1 2430]]
+[[Category: Caldanaerobacter subterraneus subsp. tengcongensis]]
 [[Category: Large Structures]]
-[[Category: Jr, C Olea]]
+[[Category: Herzik Jr MA]]
-[[Category: Jr, M A.Herzik]]
+[[Category: Kuriyan J]]
-[[Category: Kuriyan, J]]
+[[Category: Marletta MA]]
-[[Category: Marletta, M A]]
+[[Category: Olea Jr C]]
-[[Category: Signaling protein]]