1ibj
From Proteopedia
(New page: 200px<br /><applet load="1ibj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ibj, resolution 2.3Å" /> '''Crystal structure of ...) |
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| - | [[Image:1ibj.jpg|left|200px]]<br /><applet load="1ibj" size=" | + | [[Image:1ibj.jpg|left|200px]]<br /><applet load="1ibj" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ibj, resolution 2.3Å" /> | caption="1ibj, resolution 2.3Å" /> | ||
'''Crystal structure of cystathionine beta-lyase from Arabidopsis thaliana'''<br /> | '''Crystal structure of cystathionine beta-lyase from Arabidopsis thaliana'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The pyridoxal 5'-phosphate-dependent enzyme cystathionine beta-lyase (CBL) | + | The pyridoxal 5'-phosphate-dependent enzyme cystathionine beta-lyase (CBL) catalyzes the penultimate step in the de novo biosynthesis of Met in microbes and plants. Absence of CBL in higher organisms makes it an important target for the development of antibiotics and herbicides. The three-dimensional structure of cystathionine beta-lyase from Arabidopsis was determined by Patterson search techniques, using the structure of tobacco (Nicotiana tabacum) cystathionine gamma-synthase as starting point. At a resolution of 2.3 A, the model was refined to a final crystallographic R-factor of 24.9%. The overall structure is very similar to other pyridoxal 5'-phosphate-dependent enzymes of the gamma-family. Exchange of a few critical residues within the active site causes the different substrate preferences between Escherichia coli and Arabidopsis CBL. Loss of interactions at the alpha-carboxyl site is the reason for the poorer substrate binding of Arabidopsis CBL. In addition, the binding pocket of Arabidopsis CBL is larger than that of E. coli CBL, explaining the similar binding of L-cystathionine and L-djenkolate in Arabidopsis CBL in contrast to E. coli CBL, where the substrate binding site is optimized for the natural substrate cystathionine. |
==About this Structure== | ==About this Structure== | ||
| - | 1IBJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] with CO3, SO4 and PLP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cystathionine_beta-lyase Cystathionine beta-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.8 4.4.1.8] Full crystallographic information is available from [http:// | + | 1IBJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] with <scene name='pdbligand=CO3:'>CO3</scene>, <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/Cystathionine_beta-lyase Cystathionine beta-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.8 4.4.1.8] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IBJ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transsulfuration]] | [[Category: transsulfuration]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:10:07 2008'' |
Revision as of 11:10, 21 February 2008
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Crystal structure of cystathionine beta-lyase from Arabidopsis thaliana
Overview
The pyridoxal 5'-phosphate-dependent enzyme cystathionine beta-lyase (CBL) catalyzes the penultimate step in the de novo biosynthesis of Met in microbes and plants. Absence of CBL in higher organisms makes it an important target for the development of antibiotics and herbicides. The three-dimensional structure of cystathionine beta-lyase from Arabidopsis was determined by Patterson search techniques, using the structure of tobacco (Nicotiana tabacum) cystathionine gamma-synthase as starting point. At a resolution of 2.3 A, the model was refined to a final crystallographic R-factor of 24.9%. The overall structure is very similar to other pyridoxal 5'-phosphate-dependent enzymes of the gamma-family. Exchange of a few critical residues within the active site causes the different substrate preferences between Escherichia coli and Arabidopsis CBL. Loss of interactions at the alpha-carboxyl site is the reason for the poorer substrate binding of Arabidopsis CBL. In addition, the binding pocket of Arabidopsis CBL is larger than that of E. coli CBL, explaining the similar binding of L-cystathionine and L-djenkolate in Arabidopsis CBL in contrast to E. coli CBL, where the substrate binding site is optimized for the natural substrate cystathionine.
About this Structure
1IBJ is a Single protein structure of sequence from Arabidopsis thaliana with , and as ligands. Active as Cystathionine beta-lyase, with EC number 4.4.1.8 Full crystallographic information is available from OCA.
Reference
The three-dimensional structure of cystathionine beta-lyase from Arabidopsis and its substrate specificity., Breitinger U, Clausen T, Ehlert S, Huber R, Laber B, Schmidt F, Pohl E, Messerschmidt A, Plant Physiol. 2001 Jun;126(2):631-42. PMID:11402193
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