1sg3
From Proteopedia
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| , resolution 2.60Å | |||||||
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| Gene: | DAL2, ALC1, YIR029W (Saccharomyces cerevisiae) | ||||||
| Activity: | Allantoicase, with EC number 3.5.3.4 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of allantoicase
Overview
Allantoicase (EC 3.5.3.4) catalyzes the conversion of allantoate into ureidoglycolate and urea, one of the final steps in the degradation of purines to urea. The mechanism of most enzymes involved in this pathway, which has been known for a long time, is unknown. In this paper we describe the three-dimensional crystal structure of the yeast allantoicase determined at a resolution of 2.6 A by single anomalous diffraction. This constitutes the first structure for an enzyme of this pathway. The structure reveals a repeated jelly roll beta-sheet motif, also present in proteins of unrelated biochemical function. Allantoicase has a hexameric arrangement in the crystal (dimer of trimers). Analysis of the protein sequence against the structural data reveals the presence of two totally conserved surface patches, one on each jelly roll motif. The hexameric packing concentrates these patches into conserved pockets that probably constitute the active site.
About this Structure
1SG3 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Crystal structure of yeast allantoicase reveals a repeated jelly roll motif., Leulliot N, Quevillon-Cheruel S, Sorel I, Graille M, Meyer P, Liger D, Blondeau K, Janin J, van Tilbeurgh H, J Biol Chem. 2004 May 28;279(22):23447-52. Epub 2004 Mar 12. PMID:15020593
Page seeded by OCA on Thu Mar 20 14:04:26 2008
