1doc

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1doc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1doc, resolution 2.0&Aring;" /> '''THE MOBIL FLAVIN OF 4...)
Line 1: Line 1:
-
[[Image:1doc.gif|left|200px]]<br /><applet load="1doc" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1doc.gif|left|200px]]<br /><applet load="1doc" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1doc, resolution 2.0&Aring;" />
caption="1doc, resolution 2.0&Aring;" />
'''THE MOBIL FLAVIN OF 4-OH BENZOATE HYDROXYLASE: MOTION OF A PROSTHETIC GROUP REGULATES CATALYSIS'''<br />
'''THE MOBIL FLAVIN OF 4-OH BENZOATE HYDROXYLASE: MOTION OF A PROSTHETIC GROUP REGULATES CATALYSIS'''<br />
==Overview==
==Overview==
-
Para-hydroxybenzoate hydroxylase inserts oxygen into substrates by means, of the labile intermediate, flavin C(4a)-hydroperoxide. This reaction, requires transient isolation of the flavin and substrate from the bulk, solvent. Previous crystal structures have revealed the position of the, substrate para-hydroxybenzoate during oxygenation but not how it enters, the active site. In this study, enzyme structures with the flavin ring, displaced relative to the protein were determined, and it was established, that these or similar flavin conformations also occur in solution., Movement of the flavin appears to be essential for the translocation of, substrates and products into the solvent-shielded active site during, catalysis.
+
Para-hydroxybenzoate hydroxylase inserts oxygen into substrates by means of the labile intermediate, flavin C(4a)-hydroperoxide. This reaction requires transient isolation of the flavin and substrate from the bulk solvent. Previous crystal structures have revealed the position of the substrate para-hydroxybenzoate during oxygenation but not how it enters the active site. In this study, enzyme structures with the flavin ring displaced relative to the protein were determined, and it was established that these or similar flavin conformations also occur in solution. Movement of the flavin appears to be essential for the translocation of substrates and products into the solvent-shielded active site during catalysis.
==About this Structure==
==About this Structure==
-
1DOC 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 BR, FAD and PHB as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DOC OCA].
+
1DOC 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=BR:'>BR</scene>, <scene name='pdbligand=FAD:'>FAD</scene> and <scene name='pdbligand=PHB:'>PHB</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DOC OCA].
==Reference==
==Reference==
Line 13: Line 13:
[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Single protein]]
[[Category: Single protein]]
-
[[Category: Ballou, D.P.]]
+
[[Category: Ballou, D P.]]
[[Category: Entsch, B.]]
[[Category: Entsch, B.]]
-
[[Category: Gatti, D.L.]]
+
[[Category: Gatti, D L.]]
-
[[Category: Lah, M.S.]]
+
[[Category: Lah, M S.]]
-
[[Category: Ludwig, M.L.]]
+
[[Category: Ludwig, M L.]]
[[Category: Massey, V.]]
[[Category: Massey, V.]]
-
[[Category: Palfey, B.A.]]
+
[[Category: Palfey, B A.]]
[[Category: BR]]
[[Category: BR]]
[[Category: FAD]]
[[Category: FAD]]
Line 25: Line 25:
[[Category: oxidoreductase]]
[[Category: oxidoreductase]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:26:40 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:18:41 2008''

Revision as of 10:18, 21 February 2008

Image:1doc.gif

1doc, resolution 2.0Å

Drag the structure with the mouse to rotate

THE MOBIL FLAVIN OF 4-OH BENZOATE HYDROXYLASE: MOTION OF A PROSTHETIC GROUP REGULATES CATALYSIS

Overview

Para-hydroxybenzoate hydroxylase inserts oxygen into substrates by means of the labile intermediate, flavin C(4a)-hydroperoxide. This reaction requires transient isolation of the flavin and substrate from the bulk solvent. Previous crystal structures have revealed the position of the substrate para-hydroxybenzoate during oxygenation but not how it enters the active site. In this study, enzyme structures with the flavin ring displaced relative to the protein were determined, and it was established that these or similar flavin conformations also occur in solution. Movement of the flavin appears to be essential for the translocation of substrates and products into the solvent-shielded active site during catalysis.

About this Structure

1DOC is a Single protein structure of sequence from Pseudomonas aeruginosa with , and as ligands. Full crystallographic information is available from OCA.

Reference

The mobile flavin of 4-OH benzoate hydroxylase., Gatti DL, Palfey BA, Lah MS, Entsch B, Massey V, Ballou DP, Ludwig ML, Science. 1994 Oct 7;266(5182):110-4. PMID:7939628

Page seeded by OCA on Thu Feb 21 12:18:41 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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