2c14
From Proteopedia
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|PDB= 2c14 |SIZE=350|CAPTION= <scene name='initialview01'>2c14</scene>, resolution 1.90Å | |PDB= 2c14 |SIZE=350|CAPTION= <scene name='initialview01'>2c14</scene>, resolution 1.90Å | ||
|SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+B'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+B'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene> | + | |LIGAND= <scene name='pdbligand=CYJ:(Z)-N~6~-[(4R,5S)-5-(2-CARBOXYETHYL)-4-(CARBOXYMETHYL)PIPERIDIN-3-YLIDENE]-L-LYSINE'>CYJ</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <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> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c14 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c14 OCA], [http://www.ebi.ac.uk/pdbsum/2c14 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2c14 RCSB]</span> | ||
}} | }} | ||
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[[Category: Neier, R.]] | [[Category: Neier, R.]] | ||
[[Category: Nentwich, M.]] | [[Category: Nentwich, M.]] | ||
| - | [[Category: MG]] | ||
[[Category: cocrystallization]] | [[Category: cocrystallization]] | ||
[[Category: enzyme mechanism]] | [[Category: enzyme mechanism]] | ||
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[[Category: porphyrin biosynthesis]] | [[Category: porphyrin biosynthesis]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:14:48 2008'' |
Revision as of 23:14, 30 March 2008
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| , resolution 1.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , | ||||||
| Activity: | Porphobilinogen synthase, with EC number 4.2.1.24 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
5-(4-CARBOXY-2-OXO-BUTYLAMINO)-4-OXO-PENTANOIC ACID ACID BOUND TO PORPHOBILINOGEN SYNTHASE FROM PSEUDOMONAS AERUGINOSA
Overview
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.
About this Structure
2C14 is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.
Reference
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
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