1b9i
From Proteopedia
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|PDB= 1b9i |SIZE=350|CAPTION= <scene name='initialview01'>1b9i</scene>, resolution 2.0Å | |PDB= 1b9i |SIZE=350|CAPTION= <scene name='initialview01'>1b9i</scene>, resolution 2.0Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=PXG:3-[O-PHOSPHONOPYRIDOXYL]--AMINO-BENZOIC ACID'>PXG</scene> | + | |LIGAND= <scene name='pdbligand=PXG:3-[O-PHOSPHONOPYRIDOXYL]--AMINO-BENZOIC+ACID'>PXG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b9i OCA], [http://www.ebi.ac.uk/pdbsum/1b9i PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1b9i RCSB]</span> | ||
}} | }} | ||
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[[Category: Scapin, G.]] | [[Category: Scapin, G.]] | ||
[[Category: Yu, T W.]] | [[Category: Yu, T W.]] | ||
| - | [[Category: PXG]] | ||
[[Category: rifamycin biosynthesis (rifd gene)]] | [[Category: rifamycin biosynthesis (rifd gene)]] | ||
| - | ''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 18:56:23 2008'' |
Revision as of 15:56, 30 March 2008
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| , resolution 2.0Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF 3-AMINO-5-HYDROXYBENZOIC ACID (AHBA) SYNTHASE
Overview
The biosynthesis of ansamycin antibiotics, including rifamycin B, involves the synthesis of an aromatic precursor, 3-amino-5-hydroxybenzoic acid (AHBA), which serves as starter for the assembly of the antibiotics' polyketide backbone. The terminal enzyme of AHBA formation, AHBA synthase, is a dimeric, pyridoxal 5'-phosphate (PLP) dependent enzyme with pronounced sequence homology to a number of PLP enzymes involved in the biosynthesis of antibiotic sugar moieties. The structure of AHBA synthase from Amycolatopsis mediterranei has been determined to 2.0 A resolution, with bound cofactor, PLP, and in a complex with PLP and an inhibitor (gabaculine). The overall fold of AHBA synthase is similar to that of the aspartate aminotransferase family of PLP-dependent enzymes, with a large domain containing a seven-stranded beta-sheet surrounded by alpha-helices and a smaller domain consisting of a four-stranded antiparallel beta-sheet and four alpha-helices. The uninhibited form of the enzyme shows the cofactor covalently linked to Lys188 in an internal aldimine linkage. On binding the inhibitor, gabaculine, the internal aldimine linkage is broken, and a covalent bond is observed between the cofactor and inhibitor. The active site is composed of residues from two subunits of AHBA synthase, indicating that AHBA synthase is active as a dimer.
About this Structure
1B9I is a Single protein structure of sequence from Amycolatopsis mediterranei. Full crystallographic information is available from OCA.
Reference
Crystal structure of 3-amino-5-hydroxybenzoic acid (AHBA) synthase., Eads JC, Beeby M, Scapin G, Yu TW, Floss HG, Biochemistry. 1999 Aug 3;38(31):9840-9. PMID:10433690
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