2e7z
From Proteopedia
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- | [[Image:2e7z.jpg|left|200px]] | + | [[Image:2e7z.jpg|left|200px]] |
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- | '''Acetylene Hydratase from Pelobacter acetylenicus''' | + | {{Structure |
+ | |PDB= 2e7z |SIZE=350|CAPTION= <scene name='initialview01'>2e7z</scene>, resolution 1.26Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=MGD:2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE+GUANOSINE+DINUCLEOTIDE'>MGD</scene>, <scene name='pdbligand=W:TUNGSTEN+ION'>W</scene> and <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene> | ||
+ | |ACTIVITY= [http://en.wikipedia.org/wiki/Deleted_entry Deleted entry], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.71 4.2.1.71] | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''Acetylene Hydratase from Pelobacter acetylenicus''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 2E7Z is a [ | + | 2E7Z is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pelobacter_acetylenicus Pelobacter acetylenicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E7Z OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17360611 17360611] |
[[Category: Deleted entry]] | [[Category: Deleted entry]] | ||
[[Category: Pelobacter acetylenicus]] | [[Category: Pelobacter acetylenicus]] | ||
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[[Category: tungstoprotein]] | [[Category: tungstoprotein]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:36:33 2008'' |
Revision as of 14:36, 20 March 2008
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, resolution 1.26Å | |||||||
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Ligands: | , , , , and | ||||||
Activity: | Deleted entry, with EC number 4.2.1.71 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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. 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 Mar 20 16:36:33 2008
Categories: Deleted entry | Pelobacter acetylenicus | Single protein | Einsle, O. | Kroneck, P M.H. | Messerschmidt, A. | Seiffert, G B. | ACT | MGD | MPD | NA | SF4 | W | Dmso reductase family | Iron-sulfur-cluster | Tungstoprotein