View source for 2c16


==5-(4-Carboxy-2-oxo-butane-1-sulfinyl)-4-oxo-pentanoic acid acid bound to Porphobilinogen synthase from Pseudomonas aeruginosa==
<StructureSection load='2c16' size='340' side='right'caption='[[2c16]], [[Resolution|resolution]] 2.02&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2c16]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C16 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C16 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=OBS:(Z)-N^6-[(4S,5R)-5-(2-CARBOXYETHYL)-4-(CARBOXYMETHYL)-1-HYDROXYDIHYDRO-2H-THIOPYRANIUM-3(4H)-YLIDENE]-L-LYSINE'>OBS</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1b4k|1b4k]], [[1gzg|1gzg]], [[1w54|1w54]], [[1w56|1w56]], [[1w5m|1w5m]], [[1w5n|1w5n]], [[1w5o|1w5o]], [[1w5p|1w5p]], [[1w5q|1w5q]], [[2c13|2c13]], [[2c14|2c14]], [[2c15|2c15]], [[2c18|2c18]], [[2c19|2c19]]</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Porphobilinogen_synthase Porphobilinogen synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.24 4.2.1.24] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c16 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c16 OCA], [http://pdbe.org/2c16 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2c16 RCSB], [http://www.ebi.ac.uk/pdbsum/2c16 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2c16 ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/HEM2_PSEAE HEM2_PSEAE]] 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 (By similarity). 
== 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/c1/2c16_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=2c16 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Porphobilinogen synthase catalyzes the first committed step of the tetrapyrrole biosynthesis pathway. In an aldol-like condensation, two molecules of 5-aminolevulinic acid (ALA) form the first pyrrole, porphobilinogen. Newly synthesized analogues of a reaction intermediate of porphobilinogen synthase have been employed in studying the active site and the catalytic mechanism of this early enzyme of tetrapyrrole biosynthesis. This study combines structural and kinetic evaluation of the inhibition potency of these inhibitors. In addition, one of the determined protein structures provides for the first time structural evidence of a magnesium ion in the active site. From these results, we can corroborate an earlier postulated enzymatic mechanism that starts with formation of a C-C bond, linking C3 of the A-side ALA to C4 of the P-side ALA through an aldole addition. The obtained data are discussed with respect to the current literature.

Probing the active site of Pseudomonas aeruginosa porphobilinogen synthase using newly developed inhibitors.,Frere F, Nentwich M, Gacond S, Heinz DW, Neier R, Frankenberg-Dinkel N Biochemistry. 2006 Jul 11;45(27):8243-53. PMID:16819823<ref>PMID:16819823</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2c16" style="background-color:#fffaf0;"></div>

==See Also==
*[[Porphobilinogen synthase|Porphobilinogen synthase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Porphobilinogen synthase]]
[[Category: Frankenberg-Dinkel, N]]
[[Category: Frere, F]]
[[Category: Gacond, S]]
[[Category: Heinz, D W]]
[[Category: Neier, R]]
[[Category: Nentwich, M]]
[[Category: Cocrystallization]]
[[Category: Enzyme mechanism]]
[[Category: Lyase]]
[[Category: Magnesium]]
[[Category: Metal-binding]]
[[Category: Metalloenzyme]]
[[Category: Porphyrin biosynthesis]]