1gzg

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[[Image:1gzg.jpg|left|200px]]<br /><applet load="1gzg" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1gzg.jpg|left|200px]]
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caption="1gzg, resolution 1.66&Aring;" />
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'''COMPLEX OF A MG2-DEPENDENT PORPHOBILINOGEN SYNTHASE FROM PSEUDOMONAS AERUGINOSA (MUTANT D139N) WITH 5-FLUOROLEVULINIC ACID'''<br />
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{{Structure
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|PDB= 1gzg |SIZE=350|CAPTION= <scene name='initialview01'>1gzg</scene>, resolution 1.66&Aring;
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|SITE= <scene name='pdbsite=LA1:Active+Site+In+Molecule+B'>LA1</scene>
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene> and <scene name='pdbligand=LAF:5-FLUOROLEVULINIC ACID'>LAF</scene>
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|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]
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|GENE=
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}}
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'''COMPLEX OF A MG2-DEPENDENT PORPHOBILINOGEN SYNTHASE FROM PSEUDOMONAS AERUGINOSA (MUTANT D139N) WITH 5-FLUOROLEVULINIC ACID'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1GZG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=K:'>K</scene> and <scene name='pdbligand=LAF:'>LAF</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Known structural/functional Site: <scene name='pdbsite=LA1:Active+Site+In+Molecule+B'>LA1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GZG OCA].
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1GZG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GZG OCA].
==Reference==
==Reference==
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Structure of porphobilinogen synthase from Pseudomonas aeruginosa in complex with 5-fluorolevulinic acid suggests a double Schiff base mechanism., Frere F, Schubert WD, Stauffer F, Frankenberg N, Neier R, Jahn D, Heinz DW, J Mol Biol. 2002 Jul 5;320(2):237-47. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12079382 12079382]
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Structure of porphobilinogen synthase from Pseudomonas aeruginosa in complex with 5-fluorolevulinic acid suggests a double Schiff base mechanism., Frere F, Schubert WD, Stauffer F, Frankenberg N, Neier R, Jahn D, Heinz DW, J Mol Biol. 2002 Jul 5;320(2):237-47. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12079382 12079382]
[[Category: Porphobilinogen synthase]]
[[Category: Porphobilinogen synthase]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
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[[Category: lyase]]
[[Category: lyase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:55:45 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:30:05 2008''

Revision as of 09:30, 20 March 2008

Image:1gzg.jpg


PDB ID 1gzg

Drag the structure with the mouse to rotate
, resolution 1.66Å
Sites:
Ligands: , , , and
Activity: Porphobilinogen synthase, with EC number 4.2.1.24
Coordinates: save as pdb, mmCIF, xml



COMPLEX OF A MG2-DEPENDENT PORPHOBILINOGEN SYNTHASE FROM PSEUDOMONAS AERUGINOSA (MUTANT D139N) WITH 5-FLUOROLEVULINIC ACID


Overview

All natural tetrapyrroles, including hemes, chlorophylls and vitamin B12, share porphobilinogen (PBG) as a common precursor. Porphobilinogen synthase (PBGS) synthesizes PBG through the asymmetric condensation of two molecules of aminolevulinic acid (ALA). Crystal structures of PBGS from various sources confirm the presence of two distinct binding sites for each ALA molecule, termed A and P. We have solved the structure of the active-site variant D139N of the Mg2+-dependent PBGS from Pseudomonas aeruginosa in complex with the inhibitor 5-fluorolevulinic acid at high resolution. Uniquely, full occupancy of both substrate binding sites each by a single substrate-like molecule was observed. Both inhibitor molecules are covalently bound to two conserved, active-site lysine residues, Lys205 and Lys260, through Schiff bases. The active site now also contains a monovalent cation that may critically enhance enzymatic activity. Based on these structural data, we postulate a catalytic mechanism for P. aeruginosa PBGS initiated by a C-C bond formation between A and P-side ALA, followed by the formation of the intersubstrate Schiff base yielding the product PBG.

About this Structure

1GZG is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.

Reference

Structure of porphobilinogen synthase from Pseudomonas aeruginosa in complex with 5-fluorolevulinic acid suggests a double Schiff base mechanism., Frere F, Schubert WD, Stauffer F, Frankenberg N, Neier R, Jahn D, Heinz DW, J Mol Biol. 2002 Jul 5;320(2):237-47. PMID:12079382

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