1aw5: Difference between revisions

Revision as of 10:46, 2 May 2008

5-AMINOLEVULINATE DEHYDRATASE FROM SACCHAROMYCES CEREVISIAE

OverviewOverview

5-Aminolaevulinate dehydratase (ALAD) is a homo-octameric metallo-enzyme that catalyses the formation of porphobilinogen from 5-aminolaevulinic acid. The structure of the yeast enzyme has been solved to 2.3 A resolution, revealing that each subunit adopts a TIM barrel fold with a 39 residue N-terminal arm. Pairs of monomers wrap their arms around each other to form compact dimers and these associate to form a 422 symmetric octamer. All eight active sites are on the surface of the octamer and possess two lysine residues (210 and 263), one of which, Lys 263, forms a Schiff base link to the substrate. The two lysine side chains are close to two zinc binding sites one of which is formed by three cysteine residues (133, 135 and 143) while the other involves Cys 234 and His 142. ALAD has features at its active site that are common to both metallo- and Schiff base-aldolases and therefore represents an intriguing combination of both classes of enzyme. Lead ions, which inhibit ALAD potently, replace the zinc bound to the enzyme's unique triple-cysteine site.

About this StructureAbout this Structure

1AW5 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

X-ray structure of 5-aminolaevulinate dehydratase, a hybrid aldolase., Erskine PT, Senior N, Awan S, Lambert R, Lewis G, Tickle IJ, Sarwar M, Spencer P, Thomas P, Warren MJ, Shoolingin-Jordan PM, Wood SP, Cooper JB, Nat Struct Biol. 1997 Dec;4(12):1025-31. PMID:9406553 Page seeded by OCA on Fri May 2 10:46:01 2008

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

OCA

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 [[Image:1aw5.gif|left|200px]]
- {{Structure
+<!--
-|PDB= 1aw5 |SIZE=350|CAPTION= <scene name='initialview01'>1aw5</scene>, resolution 2.3&Aring;
+The line below this paragraph, containing "STRUCTURE_1aw5", creates the "Structure Box" on the page.
-|SITE= <scene name='pdbsite=CAT:LYS+263+Forms+Schiff+Base+w.+Substrate.+LYS+210+Is+Spati+...'>CAT</scene>
+You may change the PDB parameter (which sets the PDB file loaded into the applet)
-|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
+or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-|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>
+or leave the SCENE parameter empty for the default display.
-|GENE= HEM2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
+-->
-|DOMAIN=
+{{STRUCTURE_1aw5|  PDB=1aw5  |  SCENE=  }}
-|RELATEDENTRY=
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1aw5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aw5 OCA], [http://www.ebi.ac.uk/pdbsum/1aw5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1aw5 RCSB]</span>
-}}
 '''5-AMINOLEVULINATE DEHYDRATASE FROM SACCHAROMYCES CEREVISIAE'''
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 [[Category: Erskine, P T.]]
 [[Category: Wood, S P.]]
-[[Category: aldolase]]
+[[Category: Aldolase]]
-[[Category: dehydratase]]
+[[Category: Dehydratase]]
-[[Category: tetrapyrrole biosynthesis]]
+[[Category: Tetrapyrrole biosynthesis]]
-[[Category: tim-barrel octamer]]
+[[Category: Tim-barrel octamer]]
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 10:46:01 2008''
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:48:39 2008''