This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1b9h

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1b9h.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1b9h.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1b9h| PDB=1b9h | SCENE= }}
{{STRUCTURE_1b9h| PDB=1b9h | SCENE= }}
-
'''CRYSTAL STRUCTURE OF 3-AMINO-5-HYDROXYBENZOIC ACID (AHBA) SYNTHASE'''
+
===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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10433690}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10433690 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10433690}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Scapin, G.]]
[[Category: Scapin, G.]]
[[Category: Yu, T W.]]
[[Category: Yu, T W.]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:14:32 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 18:37:58 2008''

Revision as of 15:38, 30 June 2008

Template:STRUCTURE 1b9h

CRYSTAL STRUCTURE OF 3-AMINO-5-HYDROXYBENZOIC ACID (AHBA) SYNTHASE

Template:ABSTRACT PUBMED 10433690

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

Page seeded by OCA on Mon Jun 30 18:37:58 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools