1aw5: Difference between revisions

Revision as of 17:43, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1aw5.png

Template:STRUCTURE 1aw5

5-AMINOLEVULINATE DEHYDRATASE FROM SACCHAROMYCES CEREVISIAE5-AMINOLEVULINATE DEHYDRATASE FROM SACCHAROMYCES CEREVISIAE

Template:ABSTRACT PUBMED 9406553

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

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-'''5-AMINOLEVULINATE DEHYDRATASE FROM SACCHAROMYCES CEREVISIAE'''
+===5-AMINOLEVULINATE DEHYDRATASE FROM SACCHAROMYCES CEREVISIAE===
-==Overview==
+<!--
--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.
+The line below this paragraph, {{ABSTRACT_PUBMED_9406553}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_9406553}}
 ==About this Structure==
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 [[Category: Tetrapyrrole biosynthesis]]
 [[Category: Tim-barrel octamer]]
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