1b4k: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 1: Line 1:
[[Image:1b4k.gif|left|200px]]<br /><applet load="1b4k" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1b4k.gif|left|200px]]
caption="1b4k, resolution 1.67&Aring;" />
 
'''HIGH RESOLUTION CRYSTAL STRUCTURE OF A MG2-DEPENDENT 5-AMINOLEVULINIC ACID DEHYDRATASE'''<br />
{{Structure
|PDB= 1b4k |SIZE=350|CAPTION= <scene name='initialview01'>1b4k</scene>, resolution 1.67&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=LEA:LEVULINIC ACID'>LEA</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]
|GENE= HEMB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 Pseudomonas aeruginosa])
}}
 
'''HIGH RESOLUTION CRYSTAL STRUCTURE OF A MG2-DEPENDENT 5-AMINOLEVULINIC ACID DEHYDRATASE'''
 


==Overview==
==Overview==
Line 7: Line 16:


==About this Structure==
==About this Structure==
1B4K 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=SO4:'>SO4</scene>, <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=LEA:'>LEA</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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B4K OCA].  
1B4K 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=1B4K OCA].  


==Reference==
==Reference==
High resolution crystal structure of a Mg2+-dependent porphobilinogen synthase., Frankenberg N, Erskine PT, Cooper JB, Shoolingin-Jordan PM, Jahn D, Heinz DW, J Mol Biol. 1999 Jun 11;289(3):591-602. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10356331 10356331]
High resolution crystal structure of a Mg2+-dependent porphobilinogen synthase., Frankenberg N, Erskine PT, Cooper JB, Shoolingin-Jordan PM, Jahn D, Heinz DW, J Mol Biol. 1999 Jun 11;289(3):591-602. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10356331 10356331]
[[Category: Porphobilinogen synthase]]
[[Category: Porphobilinogen synthase]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
Line 25: Line 34:
[[Category: magnesium]]
[[Category: magnesium]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:51:22 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:06:09 2008''

Revision as of 11:06, 20 March 2008

File:1b4k.gif


PDB ID 1b4k

Drag the structure with the mouse to rotate
, resolution 1.67Å
Ligands: , and
Gene: HEMB (Pseudomonas aeruginosa)
Activity: Porphobilinogen synthase, with EC number 4.2.1.24
Coordinates: save as pdb, mmCIF, xml



HIGH RESOLUTION CRYSTAL STRUCTURE OF A MG2-DEPENDENT 5-AMINOLEVULINIC ACID DEHYDRATASE


OverviewOverview

Common to the biosynthesis of all known tetrapyrroles is the condensation of two molecules of 5-aminolevulinic acid to the pyrrole porphobilinogen catalyzed by the enzyme porphobilinogen synthase (PBGS). Two major classes of PBGS are known. Zn2+-dependent PBGSs are found in mammals, yeast and some bacteria including Escherichia coli, while Mg2+-dependent PBGSs are present mainly in plants and other bacteria. The crystal structure of the Mg2+-dependent PBGS from the human pathogen Pseudomonas aeruginosa in complex with the competitive inhibitor levulinic acid (LA) solved at 1.67 A resolution shows a homooctameric enzyme that consists of four asymmetric dimers. The monomers in each dimer differ from each other by having a "closed" and an "open" active site pocket. In the closed subunit, the active site is completely shielded from solvent by a well-defined lid that is partially disordered in the open subunit. A single molecule of LA binds to a mainly hydrophobic pocket in each monomer where it is covalently attached via a Schiff base to an active site lysine residue. Whereas no metal ions are found in the active site of both monomers, a single well-defined and highly hydrated Mg2+is present only in the closed form about 14 A away from the Schiff base forming nitrogen atom of the active site lysine. We conclude that the observed differences in the active sites of both monomers might be induced by Mg2+-binding to this remote site and propose a structure-based mechanism for this allosteric Mg2+in rate enhancement.

About this StructureAbout this Structure

1B4K is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.

ReferenceReference

High resolution crystal structure of a Mg2+-dependent porphobilinogen synthase., Frankenberg N, Erskine PT, Cooper JB, Shoolingin-Jordan PM, Jahn D, Heinz DW, J Mol Biol. 1999 Jun 11;289(3):591-602. PMID:10356331

Page seeded by OCA on Thu Mar 20 10:06:09 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA