1gc2
From Proteopedia
(New page: 200px<br /><applet load="1gc2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gc2, resolution 2.00Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1gc2.jpg|left|200px]]<br /><applet load="1gc2" size=" | + | [[Image:1gc2.jpg|left|200px]]<br /><applet load="1gc2" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1gc2, resolution 2.00Å" /> | caption="1gc2, resolution 2.00Å" /> | ||
'''CRYSTAL STRUCTURE OF THE PYRIDOXAL-5'-PHOSPHATE DEPENDENT L-METHIONINE GAMMA-LYASE FROM PSEUDOMONAS PUTIDA'''<br /> | '''CRYSTAL STRUCTURE OF THE PYRIDOXAL-5'-PHOSPHATE DEPENDENT L-METHIONINE GAMMA-LYASE FROM PSEUDOMONAS PUTIDA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | L-Methionine gamma-lyase (MGL) catalyzes the pyridoxal 5'-phosphate (PLP) | + | L-Methionine gamma-lyase (MGL) catalyzes the pyridoxal 5'-phosphate (PLP) dependent alpha,gamma-elimination of L-methionine. We have determined two crystal structures of MGL from Pseudomonas putida using MAD (multiwavelength anomalous diffraction) and molecular replacement methods. The structures have been refined to an R-factor of 21.1% at 2.0 and 1.7 A resolution using synchrotron radiation diffraction data. A homotetramer with 222 symmetry is built up by non-crystallographic symmetry. Two monomers associate to build the active dimer. The spatial fold of subunits, with three functionally distinct domains and their quarternary arrangement, is similar to those of L-cystathionine beta-lyase and L-cystathionine gamma-synthase from Escherichia coli. |
==About this Structure== | ==About this Structure== | ||
| - | 1GC2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Active as [http://en.wikipedia.org/wiki/Methionine_gamma-lyase Methionine gamma-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.11 4.4.1.11] Full crystallographic information is available from [http:// | + | 1GC2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Active as [http://en.wikipedia.org/wiki/Methionine_gamma-lyase Methionine gamma-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.11 4.4.1.11] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GC2 OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of the pyridoxal 5'-phosphate dependent L-methionine gamma-lyase from Pseudomonas putida., Motoshima H, Inagaki K, Kumasaka T, Furuichi M, Inoue H, Tamura T, Esaki N, Soda K, Tanaka N, Yamamoto M, Tanaka H, J Biochem | + | Crystal structure of the pyridoxal 5'-phosphate dependent L-methionine gamma-lyase from Pseudomonas putida., Motoshima H, Inagaki K, Kumasaka T, Furuichi M, Inoue H, Tamura T, Esaki N, Soda K, Tanaka N, Yamamoto M, Tanaka H, J Biochem. 2000 Sep;128(3):349-54. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10965031 10965031] |
[[Category: Methionine gamma-lyase]] | [[Category: Methionine gamma-lyase]] | ||
[[Category: Pseudomonas putida]] | [[Category: Pseudomonas putida]] | ||
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[[Category: pyridoxal-5'-phosphate]] | [[Category: pyridoxal-5'-phosphate]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:48:28 2008'' |
Revision as of 10:48, 21 February 2008
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CRYSTAL STRUCTURE OF THE PYRIDOXAL-5'-PHOSPHATE DEPENDENT L-METHIONINE GAMMA-LYASE FROM PSEUDOMONAS PUTIDA
Overview
L-Methionine gamma-lyase (MGL) catalyzes the pyridoxal 5'-phosphate (PLP) dependent alpha,gamma-elimination of L-methionine. We have determined two crystal structures of MGL from Pseudomonas putida using MAD (multiwavelength anomalous diffraction) and molecular replacement methods. The structures have been refined to an R-factor of 21.1% at 2.0 and 1.7 A resolution using synchrotron radiation diffraction data. A homotetramer with 222 symmetry is built up by non-crystallographic symmetry. Two monomers associate to build the active dimer. The spatial fold of subunits, with three functionally distinct domains and their quarternary arrangement, is similar to those of L-cystathionine beta-lyase and L-cystathionine gamma-synthase from Escherichia coli.
About this Structure
1GC2 is a Single protein structure of sequence from Pseudomonas putida. Active as Methionine gamma-lyase, with EC number 4.4.1.11 Full crystallographic information is available from OCA.
Reference
Crystal structure of the pyridoxal 5'-phosphate dependent L-methionine gamma-lyase from Pseudomonas putida., Motoshima H, Inagaki K, Kumasaka T, Furuichi M, Inoue H, Tamura T, Esaki N, Soda K, Tanaka N, Yamamoto M, Tanaka H, J Biochem. 2000 Sep;128(3):349-54. PMID:10965031
Page seeded by OCA on Thu Feb 21 12:48:28 2008
