2e7z
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 2e7z |SIZE=350|CAPTION= <scene name='initialview01'>2e7z</scene>, resolution 1.26Å | |PDB= 2e7z |SIZE=350|CAPTION= <scene name='initialview01'>2e7z</scene>, resolution 1.26Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</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=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=W:TUNGSTEN+ION'>W</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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2e7z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e7z OCA], [http://www.ebi.ac.uk/pdbsum/2e7z PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2e7z RCSB]</span> | ||
}} | }} | ||
| Line 27: | Line 30: | ||
[[Category: Messerschmidt, A.]] | [[Category: Messerschmidt, A.]] | ||
[[Category: Seiffert, G B.]] | [[Category: Seiffert, G B.]] | ||
| - | [[Category: ACT]] | ||
| - | [[Category: MGD]] | ||
| - | [[Category: MPD]] | ||
| - | [[Category: NA]] | ||
| - | [[Category: SF4]] | ||
| - | [[Category: W]] | ||
[[Category: dmso reductase family]] | [[Category: dmso reductase family]] | ||
[[Category: iron-sulfur-cluster]] | [[Category: iron-sulfur-cluster]] | ||
[[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 Mon Mar 31 02:45:06 2008'' |
Revision as of 23:45, 30 March 2008
| |||||||
| , resolution 1.26Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , , | ||||||
| Activity: | Deleted entry, with EC number 4.2.1.71 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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 Mon Mar 31 02:45:06 2008
