1b9i

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[[Image:1b9i.jpg|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1b9i", creates the "Structure Box" on the page.
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|LIGAND= <scene name='pdbligand=PXG:3-[O-PHOSPHONOPYRIDOXYL]--AMINO-BENZOIC+ACID'>PXG</scene>
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{{STRUCTURE_1b9i| PDB=1b9i | SCENE= }}
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|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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'''CRYSTAL STRUCTURE OF 3-AMINO-5-HYDROXYBENZOIC ACID (AHBA) SYNTHASE'''
'''CRYSTAL STRUCTURE OF 3-AMINO-5-HYDROXYBENZOIC ACID (AHBA) SYNTHASE'''
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[[Category: Scapin, G.]]
[[Category: Scapin, G.]]
[[Category: Yu, T W.]]
[[Category: Yu, T W.]]
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[[Category: rifamycin biosynthesis (rifd gene)]]
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Revision as of 08:14, 2 May 2008

Image:1b9i.jpg

Template:STRUCTURE 1b9i

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 Page seeded by OCA on Fri May 2 11:14:37 2008

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