1pv8: Difference between revisions

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[[Image:1pv8.jpg|left|200px]]<br /><applet load="1pv8" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1pv8.jpg|left|200px]]
caption="1pv8, resolution 2.20&Aring;" />
 
'''Crystal structure of a low activity F12L mutant of human phorphobilinogen synthase'''<br />
{{Structure
|PDB= 1pv8 |SIZE=350|CAPTION= <scene name='initialview01'>1pv8</scene>, resolution 2.20&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=PB1:3-(2-AMINOETHYL)-4-(AMINOMETHYL)HEPTANEDIOIC ACID'>PB1</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= ALAD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
}}
 
'''Crystal structure of a low activity F12L mutant of human phorphobilinogen synthase'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1PV8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=PB1:'>PB1</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=1PV8 OCA].  
1PV8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PV8 OCA].  


==Reference==
==Reference==
Control of tetrapyrrole biosynthesis by alternate quaternary forms of porphobilinogen synthase., Breinig S, Kervinen J, Stith L, Wasson AS, Fairman R, Wlodawer A, Zdanov A, Jaffe EK, Nat Struct Biol. 2003 Sep;10(9):757-63. Epub 2003 Aug 3. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12897770 12897770]
Control of tetrapyrrole biosynthesis by alternate quaternary forms of porphobilinogen synthase., Breinig S, Kervinen J, Stith L, Wasson AS, Fairman R, Wlodawer A, Zdanov A, Jaffe EK, Nat Struct Biol. 2003 Sep;10(9):757-63. Epub 2003 Aug 3. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12897770 12897770]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Porphobilinogen synthase]]
[[Category: Porphobilinogen synthase]]
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[[Category: tetrapyrrole biosynthesis]]
[[Category: tetrapyrrole biosynthesis]]


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Revision as of 14:29, 20 March 2008

File:1pv8.jpg


PDB ID 1pv8

Drag the structure with the mouse to rotate
, resolution 2.20Å
Ligands: and
Gene: ALAD (Homo sapiens)
Activity: Porphobilinogen synthase, with EC number 4.2.1.24
Coordinates: save as pdb, mmCIF, xml



Crystal structure of a low activity F12L mutant of human phorphobilinogen synthase


OverviewOverview

Porphobilinogen synthase (PBGS) catalyzes the first common step in the biosynthesis of tetrapyrroles (such as heme and chlorophyll). Although the predominant oligomeric form of this enzyme, as inferred from many crystal structures, is that of a homo-octamer, a rare human PBGS allele, F12L, reveals the presence of a hexameric form. Rearrangement of an N-terminal arm is responsible for this oligomeric switch, which results in profound changes in kinetic behavior. The structural transition between octamer and hexamer must proceed through an unparalleled equilibrium containing two different dimer structures. The allosteric magnesium, present in most PBGS, has a binding site in the octamer but not in the hexamer. The unprecedented structural rearrangement reported here relates to the allosteric regulation of PBGS and suggests that alternative PBGS oligomers may function in a magnesium-dependent regulation of tetrapyrrole biosynthesis in plants and some bacteria.

DiseaseDisease

Known diseases associated with this structure: Lead poisoning, susceptibility to OMIM:[125270], Porphyria, acute hepatic OMIM:[125270]

About this StructureAbout this Structure

1PV8 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Control of tetrapyrrole biosynthesis by alternate quaternary forms of porphobilinogen synthase., Breinig S, Kervinen J, Stith L, Wasson AS, Fairman R, Wlodawer A, Zdanov A, Jaffe EK, Nat Struct Biol. 2003 Sep;10(9):757-63. Epub 2003 Aug 3. PMID:12897770

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