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| | ==2.1 Ang structure of the dimerized PAS domain of signal transduction histidine kinase from Nostoc punctiforme PCC 73102 with homology to the H-NOXA/H-NOBA domain of the soluble guanylyl cyclase== |
| The line below this paragraph, containing "STRUCTURE_2p04", creates the "Structure Box" on the page.
| | <StructureSection load='2p04' size='340' side='right'caption='[[2p04]], [[Resolution|resolution]] 2.11Å' 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'>[[2p04]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Nostoc_punctiforme_PCC_73102 Nostoc punctiforme PCC 73102]. The January 2011 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Nitric Oxide Synthase'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2011_1 10.2210/rcsb_pdb/mom_2011_1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P04 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2P04 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]] 2.11Å</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=2p04 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p04 OCA], [https://pdbe.org/2p04 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2p04 RCSB], [https://www.ebi.ac.uk/pdbsum/2p04 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2p04 ProSAT]</span></td></tr> |
| {{STRUCTURE_2p04| PDB=2p04 | SCENE= }}
| | </table> |
| | | == Function == |
| '''2.1 Ang structure of the dimerized PAS domain of signal transduction histidine kinase from Nostoc punctiforme PCC 73102 with homology to the H-NOXA/H-NOBA domain of the soluble guanylyl cyclase'''
| | [https://www.uniprot.org/uniprot/D0VWX5_NOSP7 D0VWX5_NOSP7] |
| | | == Evolutionary Conservation == |
| | | [[Image:Consurf_key_small.gif|200px|right]] |
| ==Overview== | | Check<jmol> |
| Signal transduction histidine kinases (STHK) are key for sensing environmental stresses, crucial for cell survival, and attain their sensing ability using small molecule binding domains. The N-terminal domain in an STHK from Nostoc punctiforme is of unknown function yet is homologous to the central region in soluble guanylyl cyclase (sGC), the main receptor for nitric oxide (NO). This domain is termed H-NOXA (or H-NOBA) because it is often associated with the heme-nitric oxide/oxygen binding (H-NOX) domain. A structure-function approach was taken to investigate the role of H-NOXA in STHK and sGC. We report the 2.1 A resolution crystal structure of the dimerized H-NOXA domain of STHK, which reveals a Per-Arnt-Sim (PAS) fold. The H-NOXA monomers dimerize in a parallel arrangement juxtaposing their N-terminal helices and preceding residues. Such PAS dimerization is similar to that previously observed for EcDOS, AvNifL, and RmFixL. Deletion of 7 N-terminal residues affected dimer organization. Alanine scanning mutagenesis in sGC indicates that the H-NOXA domains of sGC could adopt a similar dimer organization. Although most putative interface mutations did decrease sGCbeta1 H-NOXA homodimerization, heterodimerization of full-length heterodimeric sGC was mostly unaffected, likely due to the additional dimerization contacts of sGC in the coiled-coil and catalytic domains. Exceptions are mutations sGCalpha1 F285A and sGCbeta1 F217A, which each caused a drastic drop in NO stimulated activity, and mutations sGCalpha1 Q368A and sGCbeta1 Q309A, which resulted in both a complete lack of activity and heterodimerization. Our structural and mutational results provide new insights into sGC and STHK dimerization and overall architecture.
| | <jmolCheckbox> |
| | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p0/2p04_consurf.spt"</scriptWhenChecked> |
| ==About this Structure== | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| 2P04 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Nostoc_punctiforme_pcc_73102 Nostoc punctiforme pcc 73102]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P04 OCA].
| | <text>to colour the structure by Evolutionary Conservation</text> |
| | | </jmolCheckbox> |
| ==Reference== | | </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=2p04 ConSurf]. |
| PAS-mediated dimerization of soluble guanylyl cyclase revealed by signal transduction histidine kinase domain crystal structure., Ma X, Sayed N, Baskaran P, Beuve A, van den Akker F, J Biol Chem. 2008 Jan 11;283(2):1167-78. Epub 2007 Nov 15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18006497 18006497]
| | <div style="clear:both"></div> |
| [[Category: Nostoc punctiforme pcc 73102]] | | __TOC__ |
| [[Category: Single protein]] | | </StructureSection> |
| [[Category: Akker, F van den.]] | | [[Category: Large Structures]] |
| [[Category: Ma, X.]] | | [[Category: Nitric Oxide Synthase]] |
| [[Category: Homologous to soluble guanylyl cyclase domain]] | | [[Category: Nostoc punctiforme PCC 73102]] |
| [[Category: Pas-like fold dimer]] | | [[Category: RCSB PDB Molecule of the Month]] |
| [[Category: Transferase]] | | [[Category: Ma X]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 24 09:26:25 2008''
| | [[Category: Van den Akker F]] |