3lai: Difference between revisions

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-{{Seed}}
-[[Image:3lai.jpg|left|200px]]
-<!--
+==Structural insights into the molecular mechanism of H-NOX activation==
-The line below this paragraph, containing "STRUCTURE_3lai", creates the "Structure Box" on the page.
+<StructureSection load='3lai' size='340' side='right'caption='[[3lai]], [[Resolution|resolution]] 2.14&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3lai]] is a 3 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=3LAI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LAI FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.144&#8491;</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>
-{{STRUCTURE_3lai|  PDB=3lai  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3lai FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lai OCA], [https://pdbe.org/3lai PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lai RCSB], [https://www.ebi.ac.uk/pdbsum/3lai PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lai ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q8RBX6_CALS4 Q8RBX6_CALS4]
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/la/3lai_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=3lai 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===
+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 3lai" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_20162612}}, adds the Publication Abstract to the page
+*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 20162612 is the PubMed ID number.
+*[[Methyl-accepting chemotaxis protein|Methyl-accepting chemotaxis protein]]
--->
+== References ==
-{{ABSTRACT_PUBMED_20162612}}
+<references/>
+__TOC__
-==About this Structure==
+</StructureSection>
-LAI is a 3 chains structure with sequences from [http://en.wikipedia.org/wiki/Thermoanaerobacter_tengcongensis Thermoanaerobacter tengcongensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LAI OCA].
+[[Category: Caldanaerobacter subterraneus subsp. tengcongensis]]
+[[Category: Large Structures]]
-==Reference==
+[[Category: Herzik Jr MA]]
-<ref group="xtra">PMID:20162612</ref><references group="xtra"/>
+[[Category: Kuriyan J]]
-[[Category: Thermoanaerobacter tengcongensis]]
+[[Category: Marletta MA]]
-[[Category: Jr, C Olea.]]
+[[Category: Olea Jr C]]
-[[Category: Jr, M A.Herzik.]]
-[[Category: Kuriyan, J.]]
-[[Category: Marletta, M A.]]
-[[Category: Signaling protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 17 09:34:42 2010''