1f2d: Difference between revisions
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|PDB= 1f2d |SIZE=350|CAPTION= <scene name='initialview01'>1f2d</scene>, resolution 2.0Å | |PDB= 1f2d |SIZE=350|CAPTION= <scene name='initialview01'>1f2d</scene>, resolution 2.0Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=PLP:PYRIDOXAL-5'-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/1-aminocyclopropane-1-carboxylate_deaminase 1-aminocyclopropane-1-carboxylate deaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.99.7 3.5.99.7] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/1-aminocyclopropane-1-carboxylate_deaminase 1-aminocyclopropane-1-carboxylate deaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.99.7 3.5.99.7] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1f2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f2d OCA], [http://www.ebi.ac.uk/pdbsum/1f2d PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1f2d RCSB]</span> | |||
}} | }} | ||
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[[Category: Yao, M.]] | [[Category: Yao, M.]] | ||
[[Category: Yokoi, D.]] | [[Category: Yokoi, D.]] | ||
[[Category: carbon-carbon lyase]] | [[Category: carbon-carbon lyase]] | ||
[[Category: open twisted alpha/beta]] | [[Category: open twisted alpha/beta]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:14:22 2008'' | ||
Revision as of 20:14, 30 March 2008
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| , resolution 2.0Å | |||||||
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| Ligands: | , | ||||||
| Activity: | 1-aminocyclopropane-1-carboxylate deaminase, with EC number 3.5.99.7 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
1-AMINOCYCLOPROPANE-1-CARBOXYLATE DEAMINASE
OverviewOverview
The pyridoxal 5'-phosphate (PLP)-dependent enzyme 1-aminocyclopropane-1-carboxylate deaminase (ACCD) catalyzes a reaction that involves a ring opening of cyclopropanoid amino acid, yielding alpha-ketobutyrate and ammonia. Unlike other PLP-dependent enzymes, this enzyme has no alpha-hydrogen atom in the substrate. Thus, a unique mechanism for the bond cleavage is expected. The crystal structure of ACCD from Hansenula saturnus has been determined at 2.0 A resolution by the multiple wavelength anomalous diffraction method using mercury atoms as anomalous scatterers. The model was built on the electron density map, which was obtained by the density averaging of multiple crystal forms. The final model was refined to an R-factor of 22.5% and an R(free)-factor of 26.8%. The ACCD folds into two domains, each of which has an open twisted alpha/beta structure similar to the beta-subunit of tryptophan synthase. However, in ACCD, unlike in other members of the beta family of PLP-dependent enzymes, PLP is buried deep in the molecule. The structure provides the first view of the catalytic center of the cyclopropane ring opening.
About this StructureAbout this Structure
1F2D is a Single protein structure of sequence from Williopsis saturnus. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of 1-aminocyclopropane-1-carboxylate deaminase from Hansenula saturnus., Yao M, Ose T, Sugimoto H, Horiuchi A, Nakagawa A, Wakatsuki S, Yokoi D, Murakami T, Honma M, Tanaka I, J Biol Chem. 2000 Nov 3;275(44):34557-65. PMID:10938279
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