2e7z: Difference between revisions
New page: left|200px<br /><applet load="2e7z" size="350" color="white" frame="true" align="right" spinBox="true" caption="2e7z, resolution 1.26Å" /> '''Acetylene Hydratase ... |
No edit summary |
||
| Line 4: | Line 4: | ||
==Overview== | ==Overview== | ||
The tungsten-iron-sulfur enzyme acetylene hydratase stands out from its | 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== | ==About this Structure== | ||
| Line 15: | Line 15: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Einsle, O.]] | [[Category: Einsle, O.]] | ||
[[Category: Kroneck, P | [[Category: Kroneck, P M.H.]] | ||
[[Category: Messerschmidt, A.]] | [[Category: Messerschmidt, A.]] | ||
[[Category: Seiffert, G | [[Category: Seiffert, G B.]] | ||
[[Category: ACT]] | [[Category: ACT]] | ||
[[Category: MGD]] | [[Category: MGD]] | ||
| Line 28: | Line 28: | ||
[[Category: tungstoprotein]] | [[Category: tungstoprotein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:07:04 2008'' | ||
Revision as of 15:07, 21 February 2008
|
Acetylene Hydratase from Pelobacter acetylenicus
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.
About this Structure
2E7Z is a Single protein structure of sequence from Pelobacter acetylenicus with NA, ACT, SF4, MGD, W and MPD as ligands. Active as Deleted entry, with EC number 4.2.1.71 Full crystallographic information is available from OCA.
Reference
Structure of the non-redox-active tungsten/[4Fe:4S] enzyme acetylene hydratase., Seiffert GB, Ullmann GM, Messerschmidt A, Schink B, Kroneck PM, Einsle O, Proc Natl Acad Sci U S A. 2007 Feb 27;104(9):3073-7. PMID:17360611
Page seeded by OCA on Thu Feb 21 17:07:04 2008
