1qgn

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|SITE=
|SITE=
|LIGAND= <scene name='pdbligand=PLP:PYRIDOXAL-5&#39;-PHOSPHATE'>PLP</scene>
|LIGAND= <scene name='pdbligand=PLP:PYRIDOXAL-5&#39;-PHOSPHATE'>PLP</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Cystathionine_gamma-synthase Cystathionine gamma-synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.48 2.5.1.48]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Cystathionine_gamma-synthase Cystathionine gamma-synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.48 2.5.1.48] </span>
|GENE= METB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4097 Nicotiana tabacum])
|GENE= METB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4097 Nicotiana tabacum])
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qgn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qgn OCA], [http://www.ebi.ac.uk/pdbsum/1qgn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qgn RCSB]</span>
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}}
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[[Category: Steegborn, C.]]
[[Category: Steegborn, C.]]
[[Category: Streber, W.]]
[[Category: Streber, W.]]
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[[Category: PLP]]
 
[[Category: gamma-family]]
[[Category: gamma-family]]
[[Category: methionine biosynthesis]]
[[Category: methionine biosynthesis]]
[[Category: pyridoxal 5'-phosphate]]
[[Category: pyridoxal 5'-phosphate]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 13:20:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:13:16 2008''

Revision as of 20:13, 30 March 2008


PDB ID 1qgn

Drag the structure with the mouse to rotate
, resolution 2.9Å
Ligands:
Gene: METB (Nicotiana tabacum)
Activity: Cystathionine gamma-synthase, with EC number 2.5.1.48
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



CYSTATHIONINE GAMMA-SYNTHASE FROM NICOTIANA TABACUM


Overview

Cystathionine gamma-synthase catalyses the committed step of de novo methionine biosynthesis in micro-organisms and plants, making the enzyme an attractive target for the design of new antibiotics and herbicides. The crystal structure of cystathionine gamma-synthase from Nicotiana tabacum has been solved by Patterson search techniques using the structure of Escherichia coli cystathionine gamma-synthase. The model was refined at 2.9 A resolution to a crystallographic R -factor of 20.1 % (Rfree25.0 %). The physiological substrates of the enzyme, L-homoserine phosphate and L-cysteine, were modelled into the unliganded structure. These complexes support the proposed ping-pong mechanism for catalysis and illustrate the dissimilar substrate specificities of bacterial and plant cystathionine gamma-synthases on a molecular level. The main difference arises from the binding modes of the distal substrate groups (O -acetyl/succinyl versusO -phosphate). Central in fixing the distal phosphate of the plant CGS substrate is an exposed lysine residue that is strictly conserved in plant cystathionine gamma-synthases whereas bacterial enzymes carry a glycine residue at this position. General insight regarding the reaction specificity of transsulphuration enzymes is gained by the comparison to cystathionine beta-lyase from E. coli, indicating the mechanistic importance of a second substrate binding site for L-cysteine which leads to different chemical reaction types.

About this Structure

1QGN is a Single protein structure of sequence from Nicotiana tabacum. Full crystallographic information is available from OCA.

Reference

The crystal structure of cystathionine gamma-synthase from Nicotiana tabacum reveals its substrate and reaction specificity., Steegborn C, Messerschmidt A, Laber B, Streber W, Huber R, Clausen T, J Mol Biol. 1999 Jul 30;290(5):983-96. PMID:10438597

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