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| | {{STRUCTURE_1ltv| PDB=1ltv | SCENE= }} | | {{STRUCTURE_1ltv| PDB=1ltv | SCENE= }} |
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| - | '''CRYSTAL STRUCTURE OF CHROMOBACTERIUM VIOLACEUM PHENYLALANINE HYDROXYLASE, STRUCTURE WITH BOUND OXIDIZED Fe(III)'''
| + | ===CRYSTAL STRUCTURE OF CHROMOBACTERIUM VIOLACEUM PHENYLALANINE HYDROXYLASE, STRUCTURE WITH BOUND OXIDIZED Fe(III)=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_12096915}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12096915 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_12096915}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Iron-bound]] | | [[Category: Iron-bound]] |
| | [[Category: Phenylalanine hydroxylase]] | | [[Category: Phenylalanine hydroxylase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:17:01 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 22:13:09 2008'' |
Revision as of 19:13, 2 July 2008
Template:STRUCTURE 1ltv
CRYSTAL STRUCTURE OF CHROMOBACTERIUM VIOLACEUM PHENYLALANINE HYDROXYLASE, STRUCTURE WITH BOUND OXIDIZED Fe(III)
Template:ABSTRACT PUBMED 12096915
About this Structure
1LTV is a Single protein structure of sequence from Chromobacterium violaceum. 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
Page seeded by OCA on Wed Jul 2 22:13:09 2008
