2e7z: Difference between revisions

Line 4:

==Overview==

The tungsten-iron-sulfur enzyme acetylene hydratase stands out from its, class because it catalyzes a nonredox reaction, the hydration of acetylene, to acetaldehyde. Sequence comparisons group the protein into the dimethyl, sulfoxide reductase family, and it contains a bis-molybdopterin guanine, dinucleotide-ligated tungsten atom and a cubane-type [4Fe:4S] cluster. The, crystal structure of acetylene hydratase at 1.26 A now shows that the, tungsten center binds a water molecule that is activated by an adjacent, aspartate residue, enabling it to attack acetylene bound in a distinct, hydrophobic pocket. This mechanism requires a strong shift of pK(a) of the, aspartate, caused by a nearby low-potential [4Fe:4S] cluster. To access, this previously unrecognized W-Asp active site, the protein evolved a new, substrate channel distant from where it is found in other molybdenum and, tungsten enzymes.

The tungsten-iron-sulfur enzyme acetylene hydratase stands out from its class because it catalyzes a nonredox reaction, the hydration of acetylene to acetaldehyde. Sequence comparisons group the protein into the dimethyl sulfoxide reductase family, and it contains a bis-molybdopterin guanine dinucleotide-ligated tungsten atom and a cubane-type [4Fe:4S] cluster. The crystal structure of acetylene hydratase at 1.26 A now shows that the tungsten center binds a water molecule that is activated by an adjacent aspartate residue, enabling it to attack acetylene bound in a distinct, hydrophobic pocket. This mechanism requires a strong shift of pK(a) of the aspartate, caused by a nearby low-potential [4Fe:4S] cluster. To access this previously unrecognized W-Asp active site, the protein evolved a new substrate channel distant from where it is found in other molybdenum and tungsten enzymes.

==About this Structure==

Line 15:

[[Category: Single protein]]

[[Category: Einsle, O.]]

[[Category: Kroneck, P.M.H.]]

[[Category: Kroneck, P M.H.]]

[[Category: Messerschmidt, A.]]

[[Category: Seiffert, G.B.]]

[[Category: Seiffert, G B.]]

[[Category: ACT]]

[[Category: MGD]]

Line 28:

[[Category: tungstoprotein]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Tue Jan 29 19~~:17:10 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:07:04 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 4: / Line 4: @@
 ==Overview==
-The tungsten-iron-sulfur enzyme acetylene hydratase stands out from its, class because it catalyzes a nonredox reaction, the hydration of acetylene, to acetaldehyde. Sequence comparisons group the protein into the dimethyl, sulfoxide reductase family, and it contains a bis-molybdopterin guanine, dinucleotide-ligated tungsten atom and a cubane-type [4Fe:4S] cluster. The, crystal structure of acetylene hydratase at 1.26 A now shows that the, tungsten center binds a water molecule that is activated by an adjacent, aspartate residue, enabling it to attack acetylene bound in a distinct, hydrophobic pocket. This mechanism requires a strong shift of pK(a) of the, aspartate, caused by a nearby low-potential [4Fe:4S] cluster. To access, this previously unrecognized W-Asp active site, the protein evolved a new, substrate channel distant from where it is found in other molybdenum and, tungsten enzymes.
+The tungsten-iron-sulfur enzyme acetylene hydratase stands out from its class because it catalyzes a nonredox reaction, the hydration of acetylene to acetaldehyde. Sequence comparisons group the protein into the dimethyl sulfoxide reductase family, and it contains a bis-molybdopterin guanine dinucleotide-ligated tungsten atom and a cubane-type [4Fe:4S] cluster. The crystal structure of acetylene hydratase at 1.26 A now shows that the tungsten center binds a water molecule that is activated by an adjacent aspartate residue, enabling it to attack acetylene bound in a distinct, hydrophobic pocket. This mechanism requires a strong shift of pK(a) of the aspartate, caused by a nearby low-potential [4Fe:4S] cluster. To access this previously unrecognized W-Asp active site, the protein evolved a new substrate channel distant from where it is found in other molybdenum and tungsten enzymes.
 ==About this Structure==
@@ Line 15: / Line 15: @@
 [[Category: Single protein]]
 [[Category: Einsle, O.]]
-[[Category: Kroneck, P.M.H.]]
+[[Category: Kroneck, P M.H.]]
 [[Category: Messerschmidt, A.]]
-[[Category: Seiffert, G.B.]]
+[[Category: Seiffert, G B.]]
 [[Category: ACT]]
 [[Category: MGD]]
@@ Line 28: / Line 28: @@
 [[Category: tungstoprotein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 19:17:10 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:07:04 2008''