1ltv
From Proteopedia
(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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| - | [[Image:1ltv.jpg|left|200px]]<br /><applet load="1ltv" size=" | + | [[Image:1ltv.jpg|left|200px]]<br /><applet load="1ltv" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ltv, resolution 2.00Å" /> | caption="1ltv, resolution 2.00Å" /> | ||
'''CRYSTAL STRUCTURE OF CHROMOBACTERIUM VIOLACEUM PHENYLALANINE HYDROXYLASE, STRUCTURE WITH BOUND OXIDIZED Fe(III)'''<br /> | '''CRYSTAL STRUCTURE OF CHROMOBACTERIUM VIOLACEUM PHENYLALANINE HYDROXYLASE, STRUCTURE WITH BOUND OXIDIZED Fe(III)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Structure determination of bacterial homologues of human disease-related | + | 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== | ==About this Structure== | ||
| - | 1LTV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Chromobacterium_violaceum Chromobacterium violaceum] with FE as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Phenylalanine_4-monooxygenase Phenylalanine 4-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.16.1 1.14.16.1] Full crystallographic information is available from [http:// | + | 1LTV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Chromobacterium_violaceum Chromobacterium violaceum] with <scene name='pdbligand=FE:'>FE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Phenylalanine_4-monooxygenase Phenylalanine 4-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.16.1 1.14.16.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LTV OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Phenylalanine 4-monooxygenase]] | [[Category: Phenylalanine 4-monooxygenase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Abu-Omar, M | + | [[Category: Abu-Omar, M M.]] |
[[Category: Erlandsen, H.]] | [[Category: Erlandsen, H.]] | ||
[[Category: Han, A.]] | [[Category: Han, A.]] | ||
| - | [[Category: Kim, J | + | [[Category: Kim, J Y.]] |
| - | [[Category: Patch, M | + | [[Category: Patch, M G.]] |
| - | [[Category: Stevens, R | + | [[Category: Stevens, R C.]] |
[[Category: Volner, A.]] | [[Category: Volner, A.]] | ||
[[Category: FE]] | [[Category: FE]] | ||
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[[Category: phenylalanine hydroxylase]] | [[Category: phenylalanine hydroxylase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:48:25 2008'' |
Revision as of 11:48, 21 February 2008
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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 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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