1gvf
From Proteopedia
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STRUCTURE OF TAGATOSE-1,6-BISPHOSPHATE ALDOLASE
Overview
Tagatose-1,6-bisphosphate aldolase (TBPA) is a tetrameric class II, aldolase that catalyzes the reversible condensation of dihydroxyacetone, phosphate with glyceraldehyde 3-phosphate to produce tagatose, 1,6-bisphosphate. The high resolution (1.45 A) crystal structure of the, Escherichia coli enzyme, encoded by the agaY gene, complexed with, phosphoglycolohydroxamate (PGH) has been determined. Two subunits comprise, the asymmetric unit, and a crystallographic 2-fold axis generates the, functional tetramer. A complex network of hydrogen bonds position side, chains in the active site that is occupied by two cations. An unusual Na+, binding site is created using a pi interaction with Tyr183 in addition to, five oxygen ligands. The catalytic Zn2+ is five-coordinate using three, histidine ... [(full description)]
About this Structure
1GVF is a [Single protein] structure of sequence from [Escherichia coli] with ZN, NA, PGH and EDO as [ligands]. Active as [Tagatose-bisphosphate aldolase], with EC number [4.1.2.40]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Structure of tagatose-1,6-bisphosphate aldolase. Insight into chiral discrimination, mechanism, and specificity of class II aldolases., Hall DR, Bond CS, Leonard GA, Watt CI, Berry A, Hunter WN, J Biol Chem. 2002 Jun 14;277(24):22018-24. Epub 2002 Apr 8. PMID:11940603
Page seeded by OCA on Tue Oct 30 15:20:22 2007
Categories: Escherichia coli | Single protein | Tagatose-bisphosphate aldolase | Hall, D.R. | Hunter, W.N. | EDO | NA | PGH | ZN | Lyase | Zinc.
