2inc: Difference between revisions

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[[Image:2inc.~~gif~~|left|200px]]

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~~'''~~Native Toluene/o-xylene Monooxygenase Hydroxylase X-ray Crystal Structure~~'''~~

===Native Toluene/o-xylene Monooxygenase Hydroxylase X-ray Crystal Structure===

~~==Overview==~~

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~~We report~~ the ~~X-ray crystal structures of native and manganese~~(~~II)-reconstituted toluene~~/~~o-xylene monooxygenase hydroxylase (ToMOH) from Pseudomonas stutzeri OX1 to 1~~.~~85 and 2~~.~~20 A resolution~~, ~~respectively. The structures reveal that reduction of the dimetallic active site~~ is ~~accompanied by a carboxylate shift and alteration of~~ the coordination environment for dioxygen binding and activation. A rotamer shift in a strategically placed asparagine 202 accompanies dimetallic center reduction and is proposed to influence protein component interactions. This rotamer shift is conserved between ToMOH and the corresponding residue in methane monooxygenase hydroxylase (MMOH). Previously unidentified hydrophobic pockets similar to those present in MMOH are assigned.

The line below this paragraph, {{ABSTRACT_PUBMED_17117860}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 17117860 is the PubMed ID number.

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==About this Structure==

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[[Category: Diiron]]

[[Category: Metalloenzyme]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun ~~May 4 07~~:41:09 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 22:21:09 2008''

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-[[Image:2inc.gif|left|200px]]
+{{Seed}}
+[[Image:2inc.png|left|200px]]
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 {{STRUCTURE_2inc|  PDB=2inc  |  SCENE=  }}
-'''Native Toluene/o-xylene Monooxygenase Hydroxylase X-ray Crystal Structure'''
+===Native Toluene/o-xylene Monooxygenase Hydroxylase X-ray Crystal Structure===
-==Overview==
+<!--
-We report the X-ray crystal structures of native and manganese(II)-reconstituted toluene/o-xylene monooxygenase hydroxylase (ToMOH) from Pseudomonas stutzeri OX1 to 1.85 and 2.20 A resolution, respectively. The structures reveal that reduction of the dimetallic active site is accompanied by a carboxylate shift and alteration of the coordination environment for dioxygen binding and activation. A rotamer shift in a strategically placed asparagine 202 accompanies dimetallic center reduction and is proposed to influence protein component interactions. This rotamer shift is conserved between ToMOH and the corresponding residue in methane monooxygenase hydroxylase (MMOH). Previously unidentified hydrophobic pockets similar to those present in MMOH are assigned.
+The line below this paragraph, {{ABSTRACT_PUBMED_17117860}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17117860 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17117860}}
 ==About this Structure==
@@ Line 30: / Line 34: @@
 [[Category: Diiron]]
 [[Category: Metalloenzyme]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 07:41:09 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 22:21:09 2008''