1p3t

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{{Seed}}
 
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[[Image:1p3t.png|left|200px]]
 
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==Crystal Structures of the NO-and CO-Bound Heme Oxygenase From Neisseria Meningitidis: Implications for Oxygen Activation==
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The line below this paragraph, containing "STRUCTURE_1p3t", creates the "Structure Box" on the page.
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<StructureSection load='1p3t' size='340' side='right'caption='[[1p3t]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1p3t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P3T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P3T FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<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></td></tr>
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{{STRUCTURE_1p3t| PDB=1p3t | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1p3t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p3t OCA], [https://pdbe.org/1p3t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p3t RCSB], [https://www.ebi.ac.uk/pdbsum/1p3t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p3t ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q9RGD9_NEIME Q9RGD9_NEIME]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p3/1p3t_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1p3t ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Heme oxygenases catalyze the oxidation of heme to biliverdin, carbon monoxide, and free iron while playing a critical role in mammalian heme homeostasis. Pathogenic bacteria such as Neisseriae meningitidis also produce heme oxygenase as part of a mechanism to mine host iron. The key step in heme oxidation is the regioselective oxidation of the heme alpha-meso-carbon by an activated Fe(III)-OOH complex. The structures of various diatomic ligands bound to the heme iron can mimic the dioxygen complex and provide important insights on the mechanism of O2 activation. Here we report the crystal structures of N. meningitidis heme oxygenase (nm-HO) in the Fe(II), Fe(II)-CO, and Fe(II)-NO states and compare these to the NO complex of human heme oxygenase-1 (Lad, L., Wang, J., Li, H., Friedman, J., Bhaskar, B., Ortiz de Montellano, P. R., and Poulos, T. L. (2003) J. Mol. Biol. 330, 527-538). Coordination of NO or CO results in a reorientation of Arg-77 that enables Arg-77 to participate in an active site H-bonded network involving a series of water molecules. One of these water molecules directly H-bonds to the Fe(II)-linked ligand and very likely serves as the proton source required for oxygen activation. Although the active site residues differ between nm-HO and human HO-1, the close similarity in the H-bonded water network suggests a common mechanism shared by all heme oxygenases.
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===Crystal Structures of the NO-and CO-Bound Heme Oxygenase From Neisseria Meningitidis: Implications for Oxygen Activation===
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Crystal structures of the NO- and CO-bound heme oxygenase from Neisseriae meningitidis. Implications for O2 activation.,Friedman J, Lad L, Deshmukh R, Li H, Wilks A, Poulos TL J Biol Chem. 2003 Sep 5;278(36):34654-9. Epub 2003 Jun 22. PMID:12819228<ref>PMID:12819228</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1p3t" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_12819228}}, adds the Publication Abstract to the page
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*[[Heme oxygenase 3D structures|Heme oxygenase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 12819228 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_12819228}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1P3T is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P3T OCA].
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==Reference==
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<ref group="xtra">PMID:12819228</ref><references group="xtra"/>
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[[Category: Heme oxygenase]]
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[[Category: Neisseria meningitidis]]
[[Category: Neisseria meningitidis]]
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[[Category: Deshmukh, R.]]
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[[Category: Deshmukh R]]
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[[Category: Friedman, J.]]
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[[Category: Friedman J]]
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[[Category: Lad, L.]]
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[[Category: Lad L]]
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[[Category: Li, H.]]
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[[Category: Li H]]
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[[Category: Poulos, T L.]]
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[[Category: Poulos TL]]
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[[Category: Wilks, A.]]
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[[Category: Wilks A]]
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[[Category: Heme degradation]]
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[[Category: Heme oxygenase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 19:40:48 2009''
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Current revision

Crystal Structures of the NO-and CO-Bound Heme Oxygenase From Neisseria Meningitidis: Implications for Oxygen Activation

PDB ID 1p3t

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