1phh: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1phh.jpg|left|200px]] | [[Image:1phh.jpg|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_1phh", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
or leave the SCENE parameter empty for the default display. | |||
| | --> | ||
| | {{STRUCTURE_1phh| PDB=1phh | SCENE= }} | ||
}} | |||
'''CRYSTAL STRUCTURE OF P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH ITS REACTION PRODUCT 3,4-DIHYDROXYBENZOATE''' | '''CRYSTAL STRUCTURE OF P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH ITS REACTION PRODUCT 3,4-DIHYDROXYBENZOATE''' | ||
| Line 28: | Line 25: | ||
[[Category: Drenth, J.]] | [[Category: Drenth, J.]] | ||
[[Category: Schreuder, H A.]] | [[Category: Schreuder, H A.]] | ||
[[Category: | [[Category: Oxidoreductase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:05:36 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 05:05, 3 May 2008
CRYSTAL STRUCTURE OF P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH ITS REACTION PRODUCT 3,4-DIHYDROXYBENZOATE
OverviewOverview
Crystals of the flavin-containing enzyme p-hydroxybenzoate hydroxylase (PHBHase) complexed with its reaction product were investigated in order to obtain insight into the catalytic cycle of this enzyme involving two substrates and two cofactors. PHBHase was crystallized initially with its substrate, p-hydroxybenzoate and the substrate was then converted into the product 3,4-dihydroxybenzoate by allowing the catalytic reaction to proceed in the crystals. In addition, crystals were soaked in mother liquor containing a high concentration of this product. Data up to 2.3 A (1 A = 0.1 nm) were collected by the oscillation method and the structure of the enzyme product complex was refined by alternate restrained least-squares procedures and model building by computer graphics techniques. A total of 273 solvent molecules could be located, four of them being presumably sulfate ions. The R-factor for 14,339 reflections between 6.0 A and 2.3 A is 19.3%. The 3-hydroxyl group of the product introduced by the enzyme is clearly visible in the electron density, showing unambiguously which carbon atom of the substrate is hydroxylated. A clear picture of the hydroxylation site is obtained. The plane of the product is rotated 21 degrees with respect to the plane of the substrate in the current model of enzyme-substrate complex. The 4-hydroxyl group of the product is hydrogen bonded to the hydroxyl group of Tyr201, its carboxyl group is interacting with the side-chains of Tyr222, Arg214 and Ser212, while the newly introduced 3-hydroxyl group makes a hydrogen bond with the backbone carbonyl oxygen of Pro293.
About this StructureAbout this Structure
1PHH is a Single protein structure of sequence from Pseudomonas fluorescens. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of p-hydroxybenzoate hydroxylase complexed with its reaction product 3,4-dihydroxybenzoate., Schreuder HA, van der Laan JM, Hol WG, Drenth J, J Mol Biol. 1988 Feb 20;199(4):637-48. PMID:3351945 Page seeded by OCA on Sat May 3 05:05:36 2008