1l8x

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{{Seed}}
 
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[[Image:1l8x.png|left|200px]]
 
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==Crystal Structure of Ferrochelatase from the Yeast, Saccharomyces cerevisiae, with Cobalt(II) as the Substrate Ion==
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The line below this paragraph, containing "STRUCTURE_1l8x", creates the "Structure Box" on the page.
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<StructureSection load='1l8x' size='340' side='right'caption='[[1l8x]], [[Resolution|resolution]] 2.70&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'>[[1l8x]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L8X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L8X 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]] 2.7&#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=CO:COBALT+(II)+ION'>CO</scene></td></tr>
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{{STRUCTURE_1l8x| PDB=1l8x | 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=1l8x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l8x OCA], [https://pdbe.org/1l8x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l8x RCSB], [https://www.ebi.ac.uk/pdbsum/1l8x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l8x ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HEMH_YEAST HEMH_YEAST] Catalyzes the ferrous insertion into protoporphyrin IX.[HAMAP-Rule:MF_00323]
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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/l8/1l8x_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=1l8x 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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Ferrochelatase is the terminal enzyme in the heme biosynthetic pathway. It catalyzes the insertion of ferrous iron into protoporphyrin IX to produce protoheme IX. The crystal structures of ferrochelatase from Saccharomyces cerevisiae in free form, in complex with Co(II), a substrate metal ion, and in complex with two inhibitors, Cd(II) and Hg(I), are presented in this work. The enzyme is a homodimer, with clear asymmetry between the monomers with regard to the porphyrin binding cleft and the mode of metal binding. The Co(II) and Cd(II) complexes reveal the metal binding site which consists of the invariant amino acids H235, E314, and S275 and solvent molecules. The shortest distance to the metal reveals that amino acid H235 is the primary metal binding residue. A second site with bound Cd(II) was found close to the surface of the molecule, approximately 14 A from H235, with E97, H317, and E326 participating in metal coordination. It is suggested that this site corresponds to the magnesium binding site in Bacillus subtilis ferrochelatase. The latter site is also located at the surface of the molecule and thought to be involved in initial metal binding and regulation.
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===Crystal Structure of Ferrochelatase from the Yeast, Saccharomyces cerevisiae, with Cobalt(II) as the Substrate Ion===
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Metal binding to Saccharomyces cerevisiae ferrochelatase.,Karlberg T, Lecerof D, Gora M, Silvegren G, Labbe-Bois R, Hansson M, Al-Karadaghi S Biochemistry. 2002 Nov 19;41(46):13499-506. PMID:12427010<ref>PMID:12427010</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 1l8x" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_12427010}}, adds the Publication Abstract to the page
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*[[Ferrochelatase 3D structures|Ferrochelatase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 12427010 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_12427010}}
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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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1L8X is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L8X OCA].
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==Reference==
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<ref group="xtra">PMID:12427010</ref><references group="xtra"/>
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[[Category: Ferrochelatase]]
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Al-Karadaghi, S.]]
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[[Category: Al-Karadaghi S]]
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[[Category: Gora, M.]]
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[[Category: Gora M]]
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[[Category: Hansson, M.]]
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[[Category: Hansson M]]
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[[Category: Karlberg, T.]]
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[[Category: Karlberg T]]
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[[Category: Labbe-Bois, R.]]
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[[Category: Labbe-Bois R]]
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[[Category: Lecerof, D.]]
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[[Category: Lecerof D]]
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[[Category: Silvegren, G.]]
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[[Category: Silvegren G]]
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[[Category: Cobalt]]
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[[Category: Ferro-lyase]]
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[[Category: Ferrochelatase]]
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[[Category: Heme biosynthesis]]
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[[Category: Mitochondrial inner membrane protein]]
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[[Category: Porphyrin metallation]]
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[[Category: Protoheme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 13:37:02 2009''
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Current revision

Crystal Structure of Ferrochelatase from the Yeast, Saccharomyces cerevisiae, with Cobalt(II) as the Substrate Ion

PDB ID 1l8x

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