1f2d
From Proteopedia
(New page: 200px<br /><applet load="1f2d" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f2d, resolution 2.0Å" /> '''1-AMINOCYCLOPROPANE-1...) |
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| - | [[Image:1f2d.jpg|left|200px]]<br /><applet load="1f2d" size=" | + | [[Image:1f2d.jpg|left|200px]]<br /><applet load="1f2d" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1f2d, resolution 2.0Å" /> | caption="1f2d, resolution 2.0Å" /> | ||
'''1-AMINOCYCLOPROPANE-1-CARBOXYLATE DEAMINASE'''<br /> | '''1-AMINOCYCLOPROPANE-1-CARBOXYLATE DEAMINASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The pyridoxal 5'-phosphate (PLP)-dependent enzyme | + | 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 Structure== | ==About this Structure== | ||
| - | 1F2D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Williopsis_saturnus Williopsis saturnus] with SO4 and PLP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 1F2D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Williopsis_saturnus Williopsis saturnus] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=PLP:'>PLP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F2D OCA]. |
==Reference== | ==Reference== | ||
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[[Category: PLP]] | [[Category: PLP]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
| - | [[Category: 1-aminocyclopropane-1-carboxylate deaminase]] | ||
[[Category: carbon-carbon lyase]] | [[Category: carbon-carbon lyase]] | ||
[[Category: open twisted alpha/beta]] | [[Category: open twisted alpha/beta]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:34:01 2008'' |
Revision as of 10:34, 21 February 2008
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1-AMINOCYCLOPROPANE-1-CARBOXYLATE DEAMINASE
Overview
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 Structure
1F2D is a Single protein structure of sequence from Williopsis saturnus with and as ligands. Active as 1-aminocyclopropane-1-carboxylate deaminase, with EC number 3.5.99.7 Full crystallographic information is available from OCA.
Reference
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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