1b9h: Difference between revisions
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'''CRYSTAL STRUCTURE OF 3-AMINO-5-HYDROXYBENZOIC ACID (AHBA) SYNTHASE''' | {{Structure | ||
|PDB= 1b9h |SIZE=350|CAPTION= <scene name='initialview01'>1b9h</scene>, resolution 2.0Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=PLP:PYRIDOXAL-5'-PHOSPHATE'>PLP</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF 3-AMINO-5-HYDROXYBENZOIC ACID (AHBA) SYNTHASE''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1B9H is a [ | 1B9H is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Amycolatopsis_mediterranei Amycolatopsis mediterranei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B9H OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10433690 10433690] | ||
[[Category: Amycolatopsis mediterranei]] | [[Category: Amycolatopsis mediterranei]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: rifamycin biosynthesis (rifd gene)]] | [[Category: rifamycin biosynthesis (rifd gene)]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:08:02 2008'' | ||
Revision as of 08:08, 20 March 2008
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| 1b9h, resolution 2.0Å | |||||||||||||
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| Ligands: | PLP | ||||||||||||
| 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
1B9H 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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