1ykj

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ykj.gif|left|200px]]<br /><applet load="1ykj" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1ykj.gif|left|200px]]
-
caption="1ykj, resolution 2.00&Aring;" />
+
 
-
'''A45G p-hydroxybenzoate hydroxylase with p-hydroxybenzoate bound'''<br />
+
{{Structure
 +
|PDB= 1ykj |SIZE=350|CAPTION= <scene name='initialview01'>1ykj</scene>, resolution 2.00&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PHB:P-HYDROXYBENZOIC+ACID'>PHB</scene> and <scene name='pdbligand=PSL:PYROSULFATE'>PSL</scene>
 +
|ACTIVITY= [http://en.wikipedia.org/wiki/4-hydroxybenzoate_3-monooxygenase 4-hydroxybenzoate 3-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.2 1.14.13.2]
 +
|GENE= pobA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 Pseudomonas aeruginosa])
 +
}}
 +
 
 +
'''A45G p-hydroxybenzoate hydroxylase with p-hydroxybenzoate bound'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1YKJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=FAD:'>FAD</scene>, <scene name='pdbligand=PHB:'>PHB</scene> and <scene name='pdbligand=PSL:'>PSL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/4-hydroxybenzoate_3-monooxygenase 4-hydroxybenzoate 3-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.2 1.14.13.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YKJ OCA].
+
1YKJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YKJ OCA].
==Reference==
==Reference==
-
Removal of a methyl group causes global changes in p-hydroxybenzoate hydroxylase., Cole LJ, Gatti DL, Entsch B, Ballou DP, Biochemistry. 2005 Jun 7;44(22):8047-58. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15924424 15924424]
+
Removal of a methyl group causes global changes in p-hydroxybenzoate hydroxylase., Cole LJ, Gatti DL, Entsch B, Ballou DP, Biochemistry. 2005 Jun 7;44(22):8047-58. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15924424 15924424]
[[Category: 4-hydroxybenzoate 3-monooxygenase]]
[[Category: 4-hydroxybenzoate 3-monooxygenase]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
Line 23: Line 32:
[[Category: SO4]]
[[Category: SO4]]
[[Category: catalysis]]
[[Category: catalysis]]
-
[[Category: conformations]]
+
[[Category: conformation]]
[[Category: phbh]]
[[Category: phbh]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:06:16 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:24:02 2008''

Revision as of 13:24, 20 March 2008

Image:1ykj.gif


PDB ID 1ykj

Drag the structure with the mouse to rotate
, resolution 2.00Å
Ligands: , , and
Gene: pobA (Pseudomonas aeruginosa)
Activity: 4-hydroxybenzoate 3-monooxygenase, with EC number 1.14.13.2
Coordinates: save as pdb, mmCIF, xml



A45G p-hydroxybenzoate hydroxylase with p-hydroxybenzoate bound


Overview

p-Hydroxybenzoate hydroxylase (PHBH) is a homodimeric flavoprotein monooxygenase that catalyzes the hydroxylation of p-hydroxybenzoate to form 3,4-dihydroxybenzoate. Controlled catalysis is achieved by movement of the flavin and protein between three conformations, in, out, and open [Entsch, B., et al. (2005) Arch. Biochem. Biophys. 433, 297-311]. The open conformation is important for substrate binding and product release, the in conformation for reaction with oxygen and hydroxylation, and the out conformation for the reduction of FAD by NADPH. The open conformation is similar to the structure of Arg220Gln-PHBH in which the backbone peptide loop of residues 43-46, located on the si side of the flavin, is rotated. In this paper, we examine the structure and properties of the Ala45Gly-PHBH mutant enzyme. The crystal structure of the Ala45Gly enzyme is an asymmetric dimer, with one monomer similar (but not identical) to wild-type PHBH, while the other monomer has His72 flipped into solvent and replaced with Glu73 as one of several changes in the structure. The two structures correlate with evidence from kinetic studies for two forms of Ala45Gly-PHBH. One form of the enzyme dominates turnover and hydroxylates, while the other contributes little to turnover and fails to hydroxylate. Ala45Gly-PHBH favors the in conformation over alternative conformations. The effect of this mutation on the structure and function of PHBH illustrates the importance of the si side loop in the conformational state of PHBH and, consequently, the function of the enzyme. This work demonstrates some general principles of how enzymes use conformational movements to allow both access and egress of substrates and product, while restricting access to the solvent at a critical stage in catalysis.

About this Structure

1YKJ is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.

Reference

Removal of a methyl group causes global changes in p-hydroxybenzoate hydroxylase., Cole LJ, Gatti DL, Entsch B, Ballou DP, Biochemistry. 2005 Jun 7;44(22):8047-58. PMID:15924424

Page seeded by OCA on Thu Mar 20 15:24:02 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ykj"
Personal tools