1ltv
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(New page: 200px<br /><applet load="1ltv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ltv, resolution 2.00Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 18:45, 20 November 2007
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CRYSTAL STRUCTURE OF CHROMOBACTERIUM VIOLACEUM PHENYLALANINE HYDROXYLASE, STRUCTURE WITH BOUND OXIDIZED Fe(III)
Overview
Structure determination of bacterial homologues of human disease-related, proteins provides an efficient path to understanding the three-dimensional, fold of proteins that are associated with human diseases. However, the, precise locations of active-site residues are often quite different, between bacterial and human versions of an enzyme, creating significant, differences in the biological understanding of enzyme homologs. To study, this hypothesis, phenylalanine hydroxylase from a bacterial source has, been structurally characterized at high resolution and comparison is made, to the human analog. The enzyme phenylalanine hydroxylase (PheOH), catalyzes the hydroxylation of l-phenylalanine into l-tyrosine utilizing, the cofactors (6R)-l-erythro-5,6,7,8 tetrahydrobiopterin (BH(4)) and, molecular oxygen. Previously determined X-ray structures of human and rat, PheOH, with a sequence identity of more than 93%, show that these two, structures are practically identical. It is thus of interest to compare, the structure of the divergent Chromobacterium violaceum phenylalanine, hydroxylase (CvPheOH) ( approximately 24% sequence identity overall) to, the related human and rat PheOH structures. We have determined crystal, structures of CvPheOH to high resolution in the apo-form (no Fe-added), Fe(III)-bound form, and 7,8-dihydro-l-biopterin (7,8-BH(2)) plus, Fe(III)-bound form. The bacterial enzyme displays higher activity and, thermal melting temperature, and structurally, differences are observed in, the N and C termini, and in a loop close to the active-site iron atom.
About this Structure
1LTV is a Single protein structure of sequence from Chromobacterium violaceum with FE as ligand. Active as Phenylalanine 4-monooxygenase, with EC number 1.14.16.1 Full crystallographic information is available from OCA.
Reference
Structural comparison of bacterial and human iron-dependent phenylalanine hydroxylases: similar fold, different stability and reaction rates., Erlandsen H, Kim JY, Patch MG, Han A, Volner A, Abu-Omar MM, Stevens RC, J Mol Biol. 2002 Jul 12;320(3):645-61. PMID:12096915
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