1gtk

From Proteopedia

Revision as of 13:14, 30 October 2007

TIME-RESOLVED AND STATIC-ENSEMBLE STRUCTURAL CHEMISTRY OF HYDROXYMETHYLBILANE SYNTHASE

Overview

The enzyme hydroxymethylbilane synthase (HMBS, EC 4.3.1.8), 313 amino acid, residues and MW 34 kDa, also known as porphobilinogen deaminase (PBGD), catalyses the stepwise polymerization of four molecules of porphobilinogen, (PBG) to the linear tetrapyrrole 1-hydroxymethylbilane. Several, crystallographic structures of HMBS have been previously determined, most, recently including by time-resolved Laue protein crystallography of the, Lys59Gln mutant form with reaction initiation undertaken by use of a flow, cell carrying the substrate PBG. In this paper we review these structures, and add new molecular graphics representations and analyses. Moreover we, present a new structure refined at 1.66 A resolution using diffraction, data recorded at cryo-temperature (100 K) in an attempt at ... [(full description)]

About this Structure

1GTK is a [Single protein] structure of sequence from [Escherichia coli] with DPM as [ligand]. Active as [Transferred entry: 2.5.1.61], with EC number [4.3.1.8]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Time-resolved and static-ensemble structural chemistry of hydroxymethylbilane synthase., Helliwell JR, Nieh YP, Habash J, Faulder PF, Raftery J, Cianci M, Wulff M, Hadener A, Faraday Discuss. 2003;122:131-44; discussion 171-90. PMID:12555854

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