1ylv

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[[Image:1ylv.jpg|left|200px]]
[[Image:1ylv.jpg|left|200px]]
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{{Structure
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|PDB= 1ylv |SIZE=350|CAPTION= <scene name='initialview01'>1ylv</scene>, resolution 2.15&Aring;
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The line below this paragraph, containing "STRUCTURE_1ylv", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=SHF:LAEVULINIC+ACID'>SHF</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|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>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1ylv| PDB=1ylv | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ylv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ylv OCA], [http://www.ebi.ac.uk/pdbsum/1ylv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ylv RCSB]</span>
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}}
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'''SCHIFF-BASE COMPLEX OF YEAST 5-AMINOLAEVULINIC ACID DEHYDRATASE WITH LAEVULINIC ACID'''
'''SCHIFF-BASE COMPLEX OF YEAST 5-AMINOLAEVULINIC ACID DEHYDRATASE WITH LAEVULINIC ACID'''
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[[Category: Warren, M J.]]
[[Category: Warren, M J.]]
[[Category: Wood, S P.]]
[[Category: Wood, S P.]]
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[[Category: aldolase]]
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[[Category: Aldolase]]
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[[Category: dehydratase]]
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[[Category: Dehydratase]]
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[[Category: tetrapyrrole synthesis]]
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[[Category: Tetrapyrrole synthesis]]
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[[Category: tim barrel]]
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[[Category: Tim barrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:29:25 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:12:37 2008''
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Revision as of 13:29, 3 May 2008

Template:STRUCTURE 1ylv

SCHIFF-BASE COMPLEX OF YEAST 5-AMINOLAEVULINIC ACID DEHYDRATASE WITH LAEVULINIC ACID


Overview

The X-ray structure of the complex formed between yeast 5-aminolaevulinic acid dehydratase (ALAD) and the inhibitor laevulinic acid has been determined at 2.15 A resolution. The inhibitor binds by forming a Schiff base link with one of the two invariant lysines at the catalytic center: Lys263. It is known that this lysine forms a Schiff base link with substrate bound at the enzyme's so-called P-site. The carboxyl group of laevulinic acid makes hydrogen bonds with the side-chain-OH groups of Tyr329 and Ser290, as well as with the main-chain >NH group of Ser290. The aliphatic moiety of the inhibitor makes hydrophobic interactions with surrounding aromatic residues in the protein including Phe219, which resides in the flap covering the active site. Our analysis strongly suggests that the same interactions will be made by P-side substrate and also indicates that the substrate that binds at the enzyme's A-site will interact with the enzyme's zinc ion bound by three cysteines (133, 135, and 143). Inhibitor binding caused a substantial ordering of the active site flap (residues 217-235), which was largely invisible in the native electron density map and indicates that this highly conserved yet flexible region has a specific role in substrate binding during catalysis.

About this Structure

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

Reference

The Schiff base complex of yeast 5-aminolaevulinic acid dehydratase with laevulinic acid., Erskine PT, Newbold R, Roper J, Coker A, Warren MJ, Shoolingin-Jordan PM, Wood SP, Cooper JB, Protein Sci. 1999 Jun;8(6):1250-6. PMID:10386874 Page seeded by OCA on Sat May 3 16:29:25 2008

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