1eb3
From Proteopedia
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|PDB= 1eb3 |SIZE=350|CAPTION= <scene name='initialview01'>1eb3</scene>, resolution 1.75Å | |PDB= 1eb3 |SIZE=350|CAPTION= <scene name='initialview01'>1eb3</scene>, resolution 1.75Å | ||
|SITE= <scene name='pdbsite=AC1:Dsb+Binding+Site+For+Chain+A'>AC1</scene> and <scene name='pdbsite=AC2:Zn+Binding+Site+For+Chain+A'>AC2</scene> | |SITE= <scene name='pdbsite=AC1:Dsb+Binding+Site+For+Chain+A'>AC1</scene> and <scene name='pdbsite=AC2:Zn+Binding+Site+For+Chain+A'>AC2</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=DSB:4,7-DIOXOSEBACIC+ACID'>DSB</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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] | + | |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> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1eb3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eb3 OCA], [http://www.ebi.ac.uk/pdbsum/1eb3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1eb3 RCSB]</span> | ||
}} | }} | ||
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[[Category: Warren, M J.]] | [[Category: Warren, M J.]] | ||
[[Category: Wood, S P.]] | [[Category: Wood, S P.]] | ||
| - | [[Category: DSB]] | ||
| - | [[Category: ZN]] | ||
[[Category: aldolase]] | [[Category: aldolase]] | ||
[[Category: dehydratase]] | [[Category: dehydratase]] | ||
| Line 40: | Line 41: | ||
[[Category: tim barrel]] | [[Category: tim barrel]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:59:04 2008'' |
Revision as of 16:59, 30 March 2008
| |||||||
| , resolution 1.75Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | and | ||||||
| Ligands: | , | ||||||
| Activity: | Porphobilinogen synthase, with EC number 4.2.1.24 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
YEAST 5-AMINOLAEVULINIC ACID DEHYDRATASE 4,7-DIOXOSEBACIC ACID COMPLEX
Overview
The structures of 5-aminolaevulinic acid dehydratase complexed with two irreversible inhibitors (4-oxosebacic acid and 4,7-dioxosebacic acid) have been solved at high resolution. Both inhibitors bind by forming a Schiff base link with Lys 263 at the active site. Previous inhibitor binding studies have defined the interactions made by only one of the two substrate moieties (P-side substrate) which bind to the enzyme during catalysis. The structures reported here provide an improved definition of the interactions made by both of the substrate molecules (A- and P-side substrates). The most intriguing result is the novel finding that 4,7-dioxosebacic acid forms a second Schiff base with the enzyme involving Lys 210. It has been known for many years that P-side substrate forms a Schiff base (with Lys 263) but until now there has been no evidence that binding of A-side substrate involves formation of a Schiff base with the enzyme. A catalytic mechanism involving substrate linked to the enzyme through Schiff bases at both the A- and P-sites is proposed.
About this Structure
1EB3 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
The X-ray structure of yeast 5-aminolaevulinic acid dehydratase complexed with two diacid inhibitors., Erskine PT, Coates L, Newbold R, Brindley AA, Stauffer F, Wood SP, Warren MJ, Cooper JB, Shoolingin-Jordan PM, Neier R, FEBS Lett. 2001 Aug 17;503(2-3):196-200. PMID:11513881
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