1gc2
From Proteopedia
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|PDB= 1gc2 |SIZE=350|CAPTION= <scene name='initialview01'>1gc2</scene>, resolution 2.00Å | |PDB= 1gc2 |SIZE=350|CAPTION= <scene name='initialview01'>1gc2</scene>, resolution 2.00Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=LLP:2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHANE)'>LLP</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1gc0|1GC0]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gc2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gc2 OCA], [http://www.ebi.ac.uk/pdbsum/1gc2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gc2 RCSB]</span> | ||
}} | }} | ||
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[[Category: pyridoxal-5'-phosphate]] | [[Category: pyridoxal-5'-phosphate]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:41:08 2008'' |
Revision as of 17:41, 30 March 2008
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| , resolution 2.00Å | |||||||
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| Ligands: | |||||||
| Activity: | Methionine gamma-lyase, with EC number 4.4.1.11 | ||||||
| Related: | 1GC0
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
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