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[[Image:2c1h.jpg|left|200px]]
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{{STRUCTURE_2c1h|  PDB=2c1h  |  SCENE=  }}
'''THE X-RAY STRUCTURE OF CHLOROBIUM VIBRIOFORME 5-AMINOLAEVULINIC ACID DEHYDRATASE COMPLEXED WITH A DIACID INHIBITOR'''


==The X-ray Structure of Chlorobium vibrioforme 5-Aminolaevulinic Acid Dehydratase Complexed with a Diacid Inhibitor==
<StructureSection load='2c1h' size='340' side='right'caption='[[2c1h]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2c1h]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Prosthecochloris_vibrioformis Prosthecochloris vibrioformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C1H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C1H FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DSB:4,7-DIOXOSEBACIC+ACID'>DSB</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=2c1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c1h OCA], [https://pdbe.org/2c1h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c1h RCSB], [https://www.ebi.ac.uk/pdbsum/2c1h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c1h ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HEM2_CHLP8 HEM2_CHLP8] Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen.
== 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/c1/2c1h_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2c1h ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The structure of Chlorobium vibrioforme 5-aminolaevulinic acid dehydratase (ALAD) complexed with the irreversible inhibitor 4,7-dioxosebacic acid has been solved. The inhibitor binds by forming Schiff-base linkages with lysines 200 and 253 at the active site. The structure reported here provides a definition of the interactions made by both of the substrate molecules (A-side and P-side substrates) with the C. vibrioforme ALAD and is compared and contrasted with structures of the same inhibitor bound to Escherichia coli and yeast ALAD. The structure suggests why 4,7-dioxosebacic acid is a better inhibitor of the zinc-dependent ALADs than of the zinc-independent ALADs.


==Overview==
Structure of Chlorobium vibrioforme 5-aminolaevulinic acid dehydratase complexed with a diacid inhibitor.,Coates L, Beaven G, Erskine PT, Beale SI, Wood SP, Shoolingin-Jordan PM, Cooper JB Acta Crystallogr D Biol Crystallogr. 2005 Dec;61(Pt 12):1594-8. Epub 2005, Nov 19. PMID:16304458<ref>PMID:16304458</ref>
The structure of Chlorobium vibrioforme 5-aminolaevulinic acid dehydratase (ALAD) complexed with the irreversible inhibitor 4,7-dioxosebacic acid has been solved. The inhibitor binds by forming Schiff-base linkages with lysines 200 and 253 at the active site. The structure reported here provides a definition of the interactions made by both of the substrate molecules (A-side and P-side substrates) with the C. vibrioforme ALAD and is compared and contrasted with structures of the same inhibitor bound to Escherichia coli and yeast ALAD. The structure suggests why 4,7-dioxosebacic acid is a better inhibitor of the zinc-dependent ALADs than of the zinc-independent ALADs.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2C1H is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Prosthecochloris_vibrioformis Prosthecochloris vibrioformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C1H OCA].
</div>
<div class="pdbe-citations 2c1h" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Structure of Chlorobium vibrioforme 5-aminolaevulinic acid dehydratase complexed with a diacid inhibitor., Coates L, Beaven G, Erskine PT, Beale SI, Wood SP, Shoolingin-Jordan PM, Cooper JB, Acta Crystallogr D Biol Crystallogr. 2005 Dec;61(Pt 12):1594-8. Epub 2005, Nov 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16304458 16304458]
*[[Porphobilinogen synthase|Porphobilinogen synthase]]
[[Category: Porphobilinogen synthase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Prosthecochloris vibrioformis]]
[[Category: Prosthecochloris vibrioformis]]
[[Category: Single protein]]
[[Category: Beale S]]
[[Category: Beale, S.]]
[[Category: Beaven G]]
[[Category: Beaven, G.]]
[[Category: Coates L]]
[[Category: Coates, L.]]
[[Category: Cooper JB]]
[[Category: Cooper, J B.]]
[[Category: Erskine PT]]
[[Category: Erskine, P T.]]
[[Category: Shoolingin-Jordan PM]]
[[Category: Shoolingin-Jordan, P M.]]
[[Category: Wood SP]]
[[Category: Wood, S P.]]
[[Category: 5-aminolaevulinic acid dehydratase]]
[[Category: Alad]]
[[Category: Heme biosynthesis]]
[[Category: Lyase]]
[[Category: Magnesium]]
[[Category: Porphyrin biosynthesis]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 21:06:17 2008''